References
- Henne WM. Organelle remodeling at membrane contact sites. J Struct Biol. 2016 Oct;196(1):15–19. DOI:https://doi.org/10.1016/j.jsb.2016.05.003.
- Bravo-Sagua R, Torrealba N, Paredes F, et al. Organelle communication: signaling crossroads between homeostasis and disease. Int J Biochem Cell Biol. 2014 May;50:55–59.
- Rossini M, Pizzo P, Filadi R. Better to keep in touch: investigating inter-organelle cross-talk. FEBS J. 2021 Feb;288(3):740–755.
- Area-Gomez E. Assessing the function of mitochondria-associated ER membranes. Methods Enzymol. 2014;547:181–197.
- Henne WM. Organelle homeostasis principles: how organelle quality control and inter-organelle crosstalk promote cell survival. Dev Cell. 2021 Apr 5;56(7):878–880. DOI:https://doi.org/10.1016/j.devcel.2021.03.012.
- Soto-Heredero G, Baixauli F, Mittelbrunn M. Interorganelle Communication between Mitochondria and the Endolysosomal System. Front Cell Dev Biol. 2017;5:95.
- Kerkhofs M, Giorgi C, Marchi S, et al. Alterations in Ca(2+) signalling via ER-mitochondria contact site remodelling in cancer. Adv Exp Med Biol. 2017;997:225–254.
- Koch GL. The endoplasmic reticulum and calcium storage. Bioessays. 1990 Nov;12(11):527–531.
- Ashby MC, Tepikin AV. ER calcium and the functions of intracellular organelles. Semin Cell Dev Biol. 2001 Feb;12(1):11–17.
- Bers DM, Perez-Reyes E. Ca channels in cardiac myocytes: structure and function in Ca influx and intracellular Ca release. Cardiovasc Res. 1999 May;42(2):339–360.
- Arruda AP, Hotamisligil GS. Calcium homeostasis and organelle function in the pathogenesis of obesity and diabetes. Cell Metab. 2015 Sep 1; 22(3):381–397. https://doi.org/10.1016/j.cmet.2015.06.010
- Raffaello A, Mammucari C, Gherardi G, et al. Calcium at the center of cell signaling: interplay between endoplasmic reticulum, mitochondria, and lysosomes. Trends Biochem Sci. 2016 Dec;41(12):1035–1049. DOI:https://doi.org/10.1016/j.tibs.2016.09.001.
- Dorn GW 2nd, Maack C. SR and mitochondria: calcium cross-talk between kissing cousins. J Mol Cell Cardiol. 2013 Feb;55:42–49. DOI:https://doi.org/10.1016/j.yjmcc.2012.07.015
- Lahiri SK, Aguilar-Sanchez Y, Wehrens XHT. Mechanisms underlying pathological Ca(2+) handling in diseases of the heart. Pflugers Arch. 2021 Mar;473(3):331–347.
- Landstrom AP, Dobrev D, Wehrens XHT. Calcium signaling and cardiac arrhythmias. Circ Res. 2017 Jun 9; 120(12):1969–1993. https://doi.org/10.1161/CIRCRESAHA.117.310083
- Eisner DA, Caldwell JL, Kistamas K, et al. Calcium and excitation-contraction coupling in the heart. Circ Res. 2017 Jul 7 121(2):181–195. https://doi.org/10.1161/CIRCRESAHA.117.310230
- Marks AR. Calcium cycling proteins and heart failure: mechanisms and therapeutics. J Clin Invest. 2013 Jan;123(1):46–52.
- Dobrev D, Wehrens XH. Role of RyR2 phosphorylation in heart failure and arrhythmias: controversies around ryanodine receptor phosphorylation in cardiac disease. Circ Res. 2014 Apr 11;114(8):1311–1319. discussion 1319 https://doi.org/10.1161/CIRCRESAHA.114.300568
- Benitah JP, Perrier R, Mercadier JJ, et al. RyR2 and Calcium release in heart failure. Front Physiol. 2021;12:734210.
- Lehnart SE, Wehrens XH, Marks AR. Calstabin deficiency, ryanodine receptors, and sudden cardiac death. Biochem Biophys Res Commun. 2004 Oct 1; 322(4):1267–1279. https://doi.org/10.1016/j.bbrc.2004.08.032
- Beavers DL, Landstrom AP, Chiang DY, et al. Emerging roles of junctophilin-2 in the heart and implications for cardiac diseases. Cardiovasc Res. 2014 Jul 15 103(2):198–205. https://doi.org/10.1093/cvr/cvu151
- Gyorke I, Hester N, Jones LR, et al. The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium. Biophys J. 2004 Apr;86(4):2121–2128. DOI:https://doi.org/10.1016/S0006-3495(04)74271-X.
- Wehrens XH, Lehnart SE, Huang F, et al. FKBP12.6 deficiency and defective calcium release channel (ryanodine receptor) function linked to exercise-induced sudden cardiac death. Cell. 2003 Jun 27 113(7):829–840. https://doi.org/10.1016/S0092-8674(03)00434-3
- van Oort Rj, Garbino A, Wang W, et al. Disrupted junctional membrane complexes and hyperactive ryanodine receptors after acute junctophilin knockdown in mice. Circulation. 2011 Mar 8 123(9):979–988. https://doi.org/10.1161/CIRCULATIONAHA.110.006437
- Reynolds JO, Quick AP, Wang Q, et al. Junctophilin-2 gene therapy rescues heart failure by normalizing RyR2-mediated Ca2+ release. Int J Cardiol. 2016 Dec 15;225:371–380. https://doi.org/10.1016/j.ijcard.2016.10.021.
- Bers DM. Ryanodine receptor S2808 phosphorylation in heart failure: smoking gun or red herring. Circ Res. 2012 Mar 16; 110(6):796–799. https://doi.org/10.1161/CIRCRESAHA.112.265579
- Marx SO, Reiken S, Hisamatsu Y, et al. PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell. 2000 May 12 101(4):365–376. https://doi.org/10.1016/S0092-8674(00)80847-8
- van Oort Rj, McCauley MD, Dixit SS, et al. Ryanodine receptor phosphorylation by calcium/calmodulin-dependent protein kinase II promotes life-threatening ventricular arrhythmias in mice with heart failure. Circulation. 2010 Dec 21 122(25):2669–2679. https://doi.org/10.1161/CIRCULATIONAHA.110.982298
- Wehrens XH, Lehnart SE, Reiken SR, et al. Ca2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor. Circ Res. 2004 Apr 2 94(6):e61–70. https://doi.org/10.1161/01.RES.0000125626.33738.E2
- Dulhunty AF, Beard NA, Hanna AD. Regulation and dysregulation of cardiac ryanodine receptor (RyR2) open probability during diastole in health and disease. J Gen Physiol. 2012 Aug;140(2):87–92.
- Sarma S, Li N, van Oort RJ, et al. Genetic inhibition of PKA phosphorylation of RyR2 prevents dystrophic cardiomyopathy. Proc Natl Acad Sci U S A. 2010 Jul 20 107(29):13165–13170. https://doi.org/10.1073/pnas.1004509107
- Shan J, Betzenhauser MJ, Kushnir A, et al. Role of chronic ryanodine receptor phosphorylation in heart failure and beta-adrenergic receptor blockade in mice. J Clin Invest. 2010 Dec;120(12):4375–4387. DOI:https://doi.org/10.1172/JCI37649.
- Li N, Wang T, Wang W, et al. Inhibition of CaMKII phosphorylation of RyR2 prevents induction of atrial fibrillation in FKBP12.6 knockout mice. Circ Res. 2012 Feb 3 110(3):465–470. https://doi.org/10.1161/CIRCRESAHA.111.253229
- Nassal D, Gratz D, Hund TJ. Challenges and opportunities for therapeutic targeting of calmodulin kinase II in heart. Front Pharmacol. 2020;11:35.
- Liu L, Liu X, Liu M, et al. Proline hydroxylase domain-containing enzymes regulate calcium levels in cardiomyocytes by TRPA1 ion channel. Exp Cell Res. 2021 Oct 15 407(2):112777. https://doi.org/10.1016/j.yexcr.2021.112777
- Campbell HM, Quick AP, Abu-Taha I, et al. Loss of SPEG inhibitory phosphorylation of ryanodine receptor type-2 promotes atrial fibrillation. Circulation. 2020 Sep 22 142(12):1159–1172. https://doi.org/10.1161/CIRCULATIONAHA.120.045791
- Alsina KM, Hulsurkar M, Brandenburg S, et al. Loss of protein phosphatase 1 regulatory subunit PPP1R3A promotes atrial fibrillation. Circulation. 2019 Aug 20 140(8):681–693. https://doi.org/10.1161/CIRCULATIONAHA.119.039642
- Chiang DY, Alsina KM, Corradini E, et al. Rearrangement of the protein phosphatase 1 Interactome during heart failure progression. Circulation. 2018 Oct 9 138(15):1569–1581. https://doi.org/10.1161/CIRCULATIONAHA.118.034361
- Little SC, Curran J, Makara MA, et al. Protein phosphatase 2A regulatory subunit B56alpha limits phosphatase activity in the heart. Sci Signal. 2015 Jul 21 8(386):ra72. https://doi.org/10.1126/scisignal.aaa5876
- Sergienko NM, Donner DG, Delbridge LMD, et al. Protein phosphatase 2A in the healthy and failing heart: new insights and therapeutic opportunities. Cell Signal. 2021 Dec 10;91:110213. https://doi.org/10.1016/j.cellsig.2021.110213.
- Kapplinger JD, Pundi KN, Larson NB, et al. Yield of the RYR2 genetic test in suspected catecholaminergic polymorphic ventricular tachycardia and implications for test interpretation. Circ Genom Precis Med. 2018 Feb;11(2):e001424. DOI:https://doi.org/10.1161/CIRCGEN.116.001424.
- Pan X, Philippen L, Lahiri SK, et al. In Vivo Ryr2 editing corrects catecholaminergic polymorphic ventricular tachycardia. Circ Res. 2018 Sep 28 123(8):953–963. https://doi.org/10.1161/CIRCRESAHA.118.313369
- Klipp RC, Li N, Wang Q, et al. EL20, a potent antiarrhythmic compound, selectively inhibits calmodulin-deficient ryanodine receptor type 2. Heart Rhythm. 2018 Apr;15(4):578–586. DOI:https://doi.org/10.1016/j.hrthm.2017.12.017.
- Connell P, Word TA, Wehrens XHT. Targeting pathological leak of ryanodine receptors: preclinical progress and the potential impact on treatments for cardiac arrhythmias and heart failure. Expert Opin Ther Targets. 2020 Jan;24(1):25–36.
- Kryshtal DO, Blackwell DJ, Egly CL, et al. RYR2 channel inhibition Is the principal mechanism of flecainide action in CPVT. Circ Res. 2021 Feb 5 128(3):321–331. https://doi.org/10.1161/CIRCRESAHA.120.316819
- Ruiz-Meana M, Minguet M, Bou-Teen D, et al. Ryanodine Receptor glycation favors mitochondrial damage in the senescent heart. Circulation. 2019 Feb 12 139(7):949–964. https://doi.org/10.1161/CIRCULATIONAHA.118.035869
- Aston D, Capel RA, Ford KL, et al. High resolution structural evidence suggests the sarcoplasmic reticulum forms microdomains with acidic stores (lysosomes) in the heart. Sci Rep. 2017 Jan 17 7(1):40620. https://doi.org/10.1038/srep40620
- Xie W, Santulli G, Reiken SR, et al. Mitochondrial oxidative stress promotes atrial fibrillation. Sci Rep. 2015 Jul 14 5(1):11427. https://doi.org/10.1038/srep11427
- Santulli G, Xie W, Reiken SR, et al. Mitochondrial calcium overload is a key determinant in heart failure. Proc Natl Acad Sci U S A. 2015 Sep 8 112(36):11389–11394. https://doi.org/10.1073/pnas.1513047112
- Chiang DY, Lahiri S, Wang G, et al. Phosphorylation-dependent interactome of ryanodine receptor type 2 in the heart. Proteomes. 2021 Jun 7 9(2):27. https://doi.org/10.3390/proteomes9020027
- Kinnear NP, Wyatt CN, Clark JH, et al. Lysosomes co-localize with ryanodine receptor subtype 3 to form a trigger zone for calcium signalling by NAADP in rat pulmonary arterial smooth muscle. Cell Calcium. 2008 Aug;44(2):190–201. DOI:https://doi.org/10.1016/j.ceca.2007.11.003.
- Gianni D, Chan J, Gwathmey JK, et al. SERCA2a in heart failure: role and therapeutic prospects. J Bioenerg Biomembr. 2005 Dec;37(6):375–380. DOI:https://doi.org/10.1007/s10863-005-9474-z.
- Kranias EG, Hajjar RJ. Modulation of cardiac contractility by the phospholamban/SERCA2a regulatome. Circ Res. 2012 Jun 8; 110(12):1646–1660. https://doi.org/10.1161/CIRCRESAHA.111.259754
- Luo W, Grupp IL, Harrer J, et al. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation. Circ Res. 1994 Sep;75(3):401–409. DOI:https://doi.org/10.1161/01.RES.75.3.401.
- Bilezikjian LM, Kranias EG, Potter JD, et al. Studies on phosphorylation of canine cardiac sarcoplasmic reticulum by calmodulin-dependent protein kinase. Circ Res. 1981 Dec;49(6):1356–1362. DOI:https://doi.org/10.1161/01.RES.49.6.1356.
- Davis BA, Edes I, Gupta RC, et al. The role of phospholamban in the regulation of calcium transport by cardiac sarcoplasmic reticulum. Mol Cell Biochem. 1990 Dec 20 99(2):83–88. https://doi.org/10.1007/BF00230337
- El-Armouche A, Pamminger T, Ditz D, et al. Decreased protein and phosphorylation level of the protein phosphatase inhibitor-1 in failing human hearts. Cardiovasc Res. 2004 Jan 1 61(1):87–93. https://doi.org/10.1016/j.cardiores.2003.11.005
- Schmitt JP, Kamisago M, Asahi M, et al. Dilated cardiomyopathy and heart failure caused by a mutation in phospholamban. Science. 2003 Feb 28 299(5611):1410–1413. https://doi.org/10.1126/science.1081578
- Haghighi K, Pritchard T, Bossuyt J, et al. The human phospholamban Arg14-deletion mutant localizes to plasma membrane and interacts with the Na/K-ATPase. J Mol Cell Cardiol. 2012 Mar;52(3):773–782. DOI:https://doi.org/10.1016/j.yjmcc.2011.11.012.
- Repetti GG, Toepfer CN, Seidman JG, et al. Novel therapies for prevention and early treatment of cardiomyopathies. Circ Res. 2019 May 24 124(11):1536–1550. https://doi.org/10.1161/CIRCRESAHA.119.313569
- Gaffin RD, Pena JR, Alves MS, et al. Long-term rescue of a familial hypertrophic cardiomyopathy caused by a mutation in the thin filament protein, tropomyosin, via modulation of a calcium cycling protein. J Mol Cell Cardiol. 2011 Nov;51(5):812–820. DOI:https://doi.org/10.1016/j.yjmcc.2011.07.026.
- Pena JR, Szkudlarek AC, Warren CM, et al. Neonatal gene transfer of Serca2a delays onset of hypertrophic remodeling and improves function in familial hypertrophic cardiomyopathy. J Mol Cell Cardiol. 2010 Dec;49(6):993–1002. DOI:https://doi.org/10.1016/j.yjmcc.2010.09.010.
- Hulot JS, Salem JE, Redheuil A, et al. Effect of intracoronary administration of AAV1/SERCA2a on ventricular remodelling in patients with advanced systolic heart failure: results from the AGENT-HF randomized phase 2 trial. Eur J Heart Fail. 2017 Nov;19(11):1534–1541. DOI:https://doi.org/10.1002/ejhf.826.
- Lyon AR, Babalis D, Morley-Smith AC, et al. Investigation of the safety and feasibility of AAV1/SERCA2a gene transfer in patients with chronic heart failure supported with a left ventricular assist device - the SERCA-LVAD TRIAL. Gene Ther. 2020 Jul 15 27(12):579–590. https://doi.org/10.1038/s41434-020-0171-7
- Carubelli V, Zhang Y, Metra M, et al. Treatment with 24 hour istaroxime infusion in patients hospitalised for acute heart failure: a randomised, placebo-controlled trial. Eur J Heart Fail. 2020 Sep;22(9):1684–1693. DOI:https://doi.org/10.1002/ejhf.1743.
- Wehrens XH. Istaroxime, a novel luso-inotropic agent for the treatment of acute heart failure. Curr Opin Invest Drugs. 2007 Sep;8(9):769–777.
- Grote Beverborg N, Spater D, Knoll R, et al. Phospholamban antisense oligonucleotides improve cardiac function in murine cardiomyopathy. Nat Commun. 2021 Aug 30 12(1):5180. https://doi.org/10.1038/s41467-021-25439-0
- Iwanaga Y, Hoshijima M, Gu Y, et al. Chronic phospholamban inhibition prevents progressive cardiac dysfunction and pathological remodeling after infarction in rats. J Clin Invest. 2004 Mar;113(5):727–736. DOI:https://doi.org/10.1172/JCI18716.
- Sahoo SK, Shaikh SA, Sopariwala DH, et al. Sarcolipin protein interaction with sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA) is distinct from phospholamban protein, and only sarcolipin can promote uncoupling of the SERCA pump. J Biol Chem. 2013 Mar 8 288(10):6881–6889. https://doi.org/10.1074/jbc.M112.436915
- Anderson DM, Anderson KM, Chang CL, et al. A micropeptide encoded by a putative long noncoding RNA regulates muscle performance. Cell. 2015 Feb 12 160(4):595–606. https://doi.org/10.1016/j.cell.2015.01.009
- Voit A, Patel V, Pachon R, et al. Reducing sarcolipin expression mitigates Duchenne muscular dystrophy and associated cardiomyopathy in mice. Nat Commun. 2017 Oct 20 8(1):1068. https://doi.org/10.1038/s41467-017-01146-7
- Kho C, Lee A, Jeong D, et al. SUMO1-dependent modulation of SERCA2a in heart failure. Nature. 2011 Sep 7 477(7366):601–605. https://doi.org/10.1038/nature10407
- Kho C, Lee A, Jeong D, et al. Small-molecule activation of SERCA2a SUMOylation for the treatment of heart failure. Nat Commun. 2015 Jun 12 6(1):7229. https://doi.org/10.1038/ncomms8229
- Quan C, Li M, Du Q, et al. SPEG Controls calcium reuptake into the sarcoplasmic reticulum through regulating SERCA2a by Its second kinase-domain. Circ Res. 2019 Mar;124(5):712–726. DOI:https://doi.org/10.1161/CIRCRESAHA.118.313916.
- Adachi T, Weisbrod RM, Pimentel DR, et al. S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nat Med. 2004 Nov;10(11):1200–1207. DOI:https://doi.org/10.1038/nm1119.
- Gorski PA, Jang SP, Jeong D, et al. Role of SIRT1 in modulating acetylation of the sarco-endoplasmic reticulum Ca(2+)-ATPase in heart failure. Circ Res. 2019 Apr 26 124(9):e63–e80. https://doi.org/10.1161/CIRCRESAHA.118.313865
- Trenker M, Malli R, Fertschai I, et al. Uncoupling proteins 2 and 3 are fundamental for mitochondrial Ca2+ uniport. Nat Cell Biol. 2007 Apr;9(4):445–452. DOI:https://doi.org/10.1038/ncb1556.
- Goodman JB, Qin F, Morgan RJ, et al. Redox-resistant SERCA [Sarco(endo)plasmic reticulum calcium atpase] attenuates oxidant-stimulated mitochondrial calcium and apoptosis in cardiac myocytes and pressure overload-induced myocardial failure in mice. Circulation. 2020 Dec 22 142(25):2459–2469. https://doi.org/10.1161/CIRCULATIONAHA.120.048183
- Ronco V, Potenza DM, Denti F, et al. A novel Ca(2)(+)-mediated cross-talk between endoplasmic reticulum and acidic organelles: implications for NAADP-dependent Ca(2)(+) signalling. Cell Calcium. 2015 Feb;57(2):89–100. DOI:https://doi.org/10.1016/j.ceca.2015.01.001.
- Garcia MI, Boehning D. Cardiac inositol 1,4,5-trisphosphate receptors. Biochim Biophys Acta Mol Cell Res. 2017 Jun;1864(6):907–914.
- Ceccarelli F, Scavuzzo MC, Giusti L, et al. ETA receptor-mediated Ca2+ mobilisation in H9c2 cardiac cells. Biochem Pharmacol. 2003 Mar 1 65(5):783–793. https://doi.org/10.1016/S0006-2952(02)01624-6
- Li X, Zima AV, Sheikh F, et al. Endothelin-1-induced arrhythmogenic Ca2+ signaling is abolished in atrial myocytes of inositol-1,4,5-trisphosphate(IP3)-receptor type 2-deficient mice. Circ Res. 2005 Jun 24 96(12):1274–1281. https://doi.org/10.1161/01.RES.0000172556.05576.4c
- Nakayama H, Bodi I, Maillet M, et al. The IP3 receptor regulates cardiac hypertrophy in response to select stimuli. Circ Res. 2010 Sep 3 107(5):659–666. https://doi.org/10.1161/CIRCRESAHA.110.220038
- Wang YJ, Huang J, Liu W, et al. IP3R-mediated Ca2+ signals govern hematopoietic and cardiac divergence of Flk1+ cells via the calcineurin-NFATc3-Etv2 pathway. J Mol Cell Biol. 2017 Aug 1 9(4):274–288. https://doi.org/10.1093/jmcb/mjx014
- Hamada K, Terauchi A, Nakamura K, et al. Aberrant calcium signaling by transglutaminase-mediated posttranslational modification of inositol 1,4,5-trisphosphate receptors. Proc Natl Acad Sci U S A. 2014 Sep 23 111(38):E3966–75. https://doi.org/10.1073/pnas.1409730111
- Garcia MI, Karlstaedt A, Chen JJ, et al. Functionally redundant control of cardiac hypertrophic signaling by inositol 1,4,5-trisphosphate receptors. J Mol Cell Cardiol. 2017 Nov;112:95–103.
- Bartok A, Weaver D, Golenar T, et al. IP3 receptor isoforms differently regulate ER-mitochondrial contacts and local calcium transfer. Nat Commun. 2019 Aug 19 10(1):3726. https://doi.org/10.1038/s41467-019-11646-3
- Xu H, Guan N, Ren YL, et al. IP3R-Grp75-VDAC1-MCU calcium regulation axis antagonists protect podocytes from apoptosis and decrease proteinuria in an Adriamycin nephropathy rat model. BMC Nephrol. 2018 Jun 15 19(1):140. https://doi.org/10.1186/s12882-018-0940-3
- Paillard M, Tubbs E, Thiebaut PA, et al. Depressing mitochondria-reticulum interactions protects cardiomyocytes from lethal hypoxia-reoxygenation injury. Circulation. 2013 Oct 1 128(14):1555–1565. https://doi.org/10.1161/CIRCULATIONAHA.113.001225
- Fazal L, Laudette M, Paula-Gomes S, et al. Multifunctional mitochondrial epac1 controls myocardial cell death. Circ Res. 2017 Feb 17 120(4):645–657. https://doi.org/10.1161/CIRCRESAHA.116.309859
- Laudette M, Coluccia A, Sainte-Marie Y, et al. Identification of a pharmacological inhibitor of Epac1 that protects the heart against acute and chronic models of cardiac stress. Cardiovasc Res. 2019 Oct 1 115(12):1766–1777. https://doi.org/10.1093/cvr/cvz076
- Thoudam T, Ha CM, Leem J, et al. PDK4 augments ER-mitochondria contact to dampen skeletal muscle insulin signaling during obesity. Diabetes. 2019 Mar;68(3):571–586. DOI:https://doi.org/10.2337/db18-0363.
- Basso V, Marchesan E, Ziviani E. A trio has turned into a quartet: DJ-1 interacts with the IP3R-Grp75-VDAC complex to control ER-mitochondria interaction. Cell Calcium. 2020 May;87:102186.
- Gomez L, Thiebaut PA, Paillard M, et al. The SR/ER-mitochondria calcium crosstalk is regulated by GSK3beta during reperfusion injury. Cell Death Differ. 2016 Feb;23(2):313–322. DOI:https://doi.org/10.1038/cdd.2015.101.
- Wu S, Lu Q, Wang Q, et al. Binding of FUN14 domain containing 1 with inositol 1,4,5-trisphosphate receptor in mitochondria-associated endoplasmic reticulum membranes Maintains mitochondrial dynamics and function in hearts in Vivo. Circulation. 2017 Dec 5 136(23):2248–2266. https://doi.org/10.1161/CIRCULATIONAHA.117.030235
- Wu S, Lu Q, Ding Y, et al. Hyperglycemia-driven inhibition of AMP-activated protein kinase alpha2 induces diabetic cardiomyopathy by promoting mitochondria-associated endoplasmic reticulum membranes In Vivo. Circulation. 2019 Apr 16 139(16):1913–1936. https://doi.org/10.1161/CIRCULATIONAHA.118.033552
- Cardenas C, Miller RA, Smith I, et al. Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca2+ transfer to mitochondria. Cell. 2010 Jul 23 142(2):270–283. https://doi.org/10.1016/j.cell.2010.06.007
- Boehning D, Joseph SK. Functional properties of recombinant type I and type III inositol 1, 4,5-trisphosphate receptor isoforms expressed in COS-7 cells. J Biol Chem. 2000 Jul 14; 275(28):21492–21499. https://doi.org/10.1074/jbc.M001724200
- Ahumada-Castro U, Bustos G, Silva-Pavez E, et al. In the right place at the right time: regulation of cell metabolism by IP3R-mediated inter-organelle Ca(2+) Fluxes. Front Cell Dev Biol. 2021;9:629522.
- Atakpa P, Thillaiappan NB, Mataragka S, et al. IP3 Receptors preferentially associate with er-lysosome contact sites and selectively deliver Ca(2+) to lysosomes. Cell Rep. 2018 Dec 11 25(11):3180–3193 e7. https://doi.org/10.1016/j.celrep.2018.11.064
- Garrity AG, Wang W, Collier CM, et al. The endoplasmic reticulum, not the pH gradient, drives calcium refilling of lysosomes. Elife. 2016 May 23;5: https://doi.org/10.7554/eLife.15887
- Karch J, Bround MJ, Khalil H, et al. Inhibition of mitochondrial permeability transition by deletion of the ANT family and CypD. Sci Adv. 2019 Aug;5(8):eaaw4597. DOI:https://doi.org/10.1126/sciadv.aaw4597.
- Kwong JQ, Molkentin JD. Physiological and pathological roles of the mitochondrial permeability transition pore in the heart. Cell Metab. 2015 Feb 3; 21(2):206–214. https://doi.org/10.1016/j.cmet.2014.12.001
- Halestrap AP, Pasdois P. The role of the mitochondrial permeability transition pore in heart disease. Biochim Biophys Acta. 2009 Nov;1787(11):1402–1415.
- Luongo TS, Lambert JP, Gross P, et al. The mitochondrial Na(+)/Ca(2+) exchanger is essential for Ca(2+) homeostasis and viability. Nature. 2017 May 4 545(7652):93–97. https://doi.org/10.1038/nature22082
- La Fuente S D, Fernandez-Sanz C, Vail C, et al. Strategic positioning and biased activity of the mitochondrial calcium uniporter in cardiac muscle. J Biol Chem. 2016 Oct 28 291(44):23343–23362. https://doi.org/10.1074/jbc.M116.755496
- La Fuente S D, Lambert JP, Nichtova Z, et al. Spatial separation of mitochondrial calcium uptake and extrusion for energy-efficient mitochondrial calcium signaling in the heart. Cell Rep. 2018 Sep 18 24(12):3099–3107 e4. https://doi.org/10.1016/j.celrep.2018.08.040
- Bonora M, Giorgi C, Pinton P. Molecular mechanisms and consequences of mitochondrial permeability transition. Nat Rev Mol Cell Biol. 2022 Apr;23(4):266–285.
- Nguyen BY, Ruiz-Velasco A, Bui T, et al. Mitochondrial function in the heart: the insight into mechanisms and therapeutic potentials. Br J Pharmacol. 2019 Nov;176(22):4302–4318. DOI:https://doi.org/10.1111/bph.14431.
- Katoshevski T, Ben-Kasus Nissim T, Sekler I. Recent studies on NCLX in health and diseases. Cell Calcium. 2021 Mar;94:102345.
- Takeuchi A, Matsuoka S. Physiological and pathophysiological roles of mitochondrial Na(+)-Ca(2+) exchanger, NCLX, in hearts. Biomolecules. 2021 Dec 14; 11(12):1876. https://doi.org/10.3390/biom11121876
- Sasaki K, Donthamsetty R, Heldak M, et al. VDAC: old protein with new roles in diabetes. Am J Physiol Cell Physiol. 2012 Nov 15 303(10):C1055–60. https://doi.org/10.1152/ajpcell.00087.2012
- Lopez-Diez R, Egana-Gorrono L, Senatus L, et al. Diabetes and cardiovascular complications: the epidemics continue. Curr Cardiol Rep. 2021 Jun 3 23(7):74. https://doi.org/10.1007/s11886-021-01504-4
- Kirkman DL, Robinson AT, Rossman MJ, et al. Mitochondrial contributions to vascular endothelial dysfunction, arterial stiffness, and cardiovascular diseases. Am J Physiol Heart Circ Physiol. 2021 May 1 320(5):H2080–H2100. https://doi.org/10.1152/ajpheart.00917.2020
- Gincel D, Zaid H, Shoshan-Barmatz V. Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function. Biochem J. 2001 Aug 15; 358(Pt 1):147–155. https://doi.org/10.1042/bj3580147
- Sampson MJ, Lovell RS, Craigen WJ. Isolation, characterization, and mapping of two mouse mitochondrial voltage-dependent anion channel isoforms. Genomics. 1996 Apr 15; 33(2):283–288. https://doi.org/10.1006/geno.1996.0193
- Zinghirino F, Pappalardo XG, Messina A, et al. Is the secret of VDAC Isoforms in their gene regulation? Characterization of human VDAC genes expression profile, promoter activity, and transcriptional regulators. Int J Mol Sci. 2020 Oct 7 21(19):7388. https://doi.org/10.3390/ijms21197388
- Ha H, Hajek P, Bedwell DM, et al. A mitochondrial porin cDNA predicts the existence of multiple human porins. J Biol Chem. 1993 Jun 5 268(16):12143–12149. https://doi.org/10.1016/S0021-9258(19)50319-2
- Queralt-Martin M, Hoogerheide DP, Noskov SY, et al. VDAC Gating thermodynamics, but not gating kinetics, are virtually temperature independent. Biophys J. 2020 Dec 15 119(12):2584–2592. https://doi.org/10.1016/j.bpj.2020.10.039
- Varughese JT, Buchanan SK, Pitt AS. The role of voltage-dependent anion channel in mitochondrial dysfunction and human disease. Cells. 2021 Jul 9; 10(7):1737. https://doi.org/10.3390/cells10071737
- Okazaki M, Kurabayashi K, Asanuma M, et al. VDAC3 gating is activated by suppression of disulfide-bond formation between the N-terminal region and the bottom of the pore. Biochim Biophys Acta. 2015 Dec;1848(12):3188–3196. DOI:https://doi.org/10.1016/j.bbamem.2015.09.017.
- Checchetto V, Reina S, Magri A, et al. Recombinant human voltage dependent anion selective channel isoform 3 (hVDAC3) forms pores with a very small conductance. Cell Physiol Biochem. 2014;34(3):842–853. DOI:https://doi.org/10.1159/000363047.
- Sander P, Gudermann T, Schredelseker J. A calcium guard in the outer membrane: is VDAC a regulated gatekeeper of mitochondrial calcium uptake? Int J Mol Sci. 2021 Jan 19; 22(2):946. https://doi.org/10.3390/ijms22020946
- Ferens FG, Summers WAT, Bharaj A, et al. A C-terminally truncated variant of neurospora crassa VDAC assembles into a partially functional form in the mitochondrial outer membrane and forms multimers in vitro. Front Physiol. 2021;12:739001.
- Choudhary OP, Paz A, Adelman JL, et al. Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1. Nat Struct Mol Biol. 2014 Jul;21(7):626–632. DOI:https://doi.org/10.1038/nsmb.2841.
- Bathori G, Csordas G, Garcia-Perez C, et al. Ca2+-dependent control of the permeability properties of the mitochondrial outer membrane and voltage-dependent anion-selective channel (VDAC). J Biol Chem. 2006 Jun 23 281(25):17347–17358. https://doi.org/10.1074/jbc.M600906200
- Zhang P, Konja D, Zhang Y, et al. Communications between mitochondria and endoplasmic reticulum in the regulation of metabolic homeostasis. Cells. 2021 Aug 25 10(9):2195. https://doi.org/10.3390/cells10092195
- Rosencrans WM, Rajendran M, Bezrukov SM, et al. VDAC regulation of mitochondrial calcium flux: from channel biophysics to disease. Cell Calcium. 2021 Mar;94:102356.
- Dia M, Gomez L, Thibault H, et al. Reduced reticulum-mitochondria Ca(2+) transfer is an early and reversible trigger of mitochondrial dysfunctions in diabetic cardiomyopathy. Basic Res Cardiol. 2020 Nov 30 115(6):74. https://doi.org/10.1007/s00395-020-00835-7
- Gonzalez-Gronow M, Gopal U, Austin RC, et al. Glucose-regulated protein (GRP78) is an important cell surface receptor for viral invasion, cancers, and neurological disorders. IUBMB Life. 2021 Jun;73(6):843–854. DOI:https://doi.org/10.1002/iub.2502.
- Ravi B, Kanwar P, Sanyal SK, et al. VDACs: an Outlook on biochemical regulation and function in animal and plant systems. Front Physiol. 2021;12:683920.
- Chaanine AH, Gordon RE, Kohlbrenner E, et al. Potential role of BNIP3 in cardiac remodeling, myocardial stiffness, and endoplasmic reticulum: mitochondrial calcium homeostasis in diastolic and systolic heart failure. Circ Heart Fail. 2013 May;6(3):572–583. DOI:https://doi.org/10.1161/CIRCHEARTFAILURE.112.000200.
- Sun X, Alford J, Qiu H. Structural and functional remodeling of mitochondria in cardiac diseases. Int J Mol Sci. 2021 Apr 17;22(8):4167.
- Camara AK, Lesnefsky EJ, Stowe DF. Potential therapeutic benefits of strategies directed to mitochondria. Antioxid Redox Signal. 2010 Aug 1; 13(3):279–347. https://doi.org/10.1089/ars.2009.2788
- Santin Y, Fazal L, Sainte-Marie Y, et al. Mitochondrial 4-HNE derived from MAO-A promotes mitoCa(2+) overload in chronic postischemic cardiac remodeling. Cell Death Differ. 2020 Jun;27(6):1907–1923. DOI:https://doi.org/10.1038/s41418-019-0470-y.
- Liao Z, Liu D, Tang L, et al. Long-term oral resveratrol intake provides nutritional preconditioning against myocardial ischemia/reperfusion injury: involvement of VDAC1 downregulation. Mol Nutr Food Res. 2015 Mar;59(3):454–464. DOI:https://doi.org/10.1002/mnfr.201400730.
- Tong Z, Xie Y, He M, et al. VDAC1 deacetylation is involved in the protective effects of resveratrol against mitochondria-mediated apoptosis in cardiomyocytes subjected to anoxia/reoxygenation injury. Biomed Pharmacother. 2017 Nov;95:77–83.
- Lin D, Cui B, Ren J, et al. Regulation of VDAC1 contributes to the cardioprotective effects of penehyclidine hydrochloride during myocardial ischemia/reperfusion. Exp Cell Res. 2018 Jun 15 367(2):257–263. https://doi.org/10.1016/j.yexcr.2018.04.004
- He H, Wang L, Qiao Y, et al. Vinegar/Tetramethylpyrazine induces nutritional preconditioning protecting the myocardium mediated by VDAC1. Oxid Med Cell Longev. 2021;2021:6670088.
- Klapper-Goldstein H, Verma A, Elyagon S, et al. VDAC1 in the diseased myocardium and the effect of VDAC1-interacting compound on atrial fibrosis induced by hyperaldosteronism. Sci Rep. 2020 Dec 16 10(1):22101. https://doi.org/10.1038/s41598-020-79056-w
- Shimada BK, Alfulaij N, Seale LA. The impact of selenium deficiency on cardiovascular function. Int J Mol Sci. 2021 Oct 2; 22(19):10713. https://doi.org/10.3390/ijms221910713
- Liu JC, Parks RJ, Liu J, et al. The In Vivo biology of the mitochondrial calcium uniporter. Adv Exp Med Biol. 2017;982:49–63.
- Kwong JQ. The mitochondrial calcium uniporter in the heart: energetics and beyond. J Physiol. 2017 Jun 15; 595(12):3743–3751. https://doi.org/10.1113/JP273059
- Baughman JM, Perocchi F, Girgis HS, et al. Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter. Nature. 2011 Jun 19 476(7360):341–345. https://doi.org/10.1038/nature10234
- De Stefani D, Raffaello A, Teardo E, et al. A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature. 2011 Jun 19 476(7360):336–340. https://doi.org/10.1038/nature10230
- Raffaello A, De Stefani D, Sabbadin D, et al. The mitochondrial calcium uniporter is a multimer that can include a dominant-negative pore-forming subunit. EMBO J. 2013 Aug 28 32(17):2362–2376. https://doi.org/10.1038/emboj.2013.157
- Sancak Y, Markhard AL, Kitami T, et al. EMRE is an essential component of the mitochondrial calcium uniporter complex. Science. 2013 Dec 13 342(6164):1379–1382. https://doi.org/10.1126/science.1242993
- Kamer KJ, Mootha VK. MICU1 and MICU2 play nonredundant roles in the regulation of the mitochondrial calcium uniporter. EMBO Rep. 2014 Mar;15(3):299–307.
- Bick AG, Calvo SE, Mootha VK. Evolutionary diversity of the mitochondrial calcium uniporter. Science. 2012 May 18; 336(6083):886. https://doi.org/10.1126/science.1214977
- Cao C, Wang S, Cui T, et al. Ion and inhibitor binding of the double-ring ion selectivity filter of the mitochondrial calcium uniporter. Proc Natl Acad Sci U S A. 2017 Apr 4 114(14):E2846–E2851. https://doi.org/10.1073/pnas.1620316114
- De Stefani D, Rizzuto R, Pozzan T. Enjoy the Trip: calcium in mitochondria back and forth. Annu Rev Biochem. 2016 Jun 2; 85(1):161–192. https://doi.org/10.1146/annurev-biochem-060614-034216
- Chaudhuri D, Sancak Y, Mootha VK, et al. MCU encodes the pore conducting mitochondrial calcium currents. Elife. 2013 Jun 4;2:e00704. https://doi.org/10.7554/eLife.00704.
- Huo J, Lu S, Kwong JQ, et al. MCUb induction protects the heart from postischemic remodeling. Circ Res. 2020 Jul 17 127(3):379–390. https://doi.org/10.1161/CIRCRESAHA.119.316369
- Patron M, Checchetto V, Raffaello A, et al. MICU1 and MICU2 finely tune the mitochondrial Ca2+ uniporter by exerting opposite effects on MCU activity. Mol Cell. 2014 Mar 6 53(5):726–737. https://doi.org/10.1016/j.molcel.2014.01.013
- Csordas G, Golenar T, Seifert EL, et al. MICU1 controls both the threshold and cooperative activation of the mitochondrial Ca(2)(+) uniporter. Cell Metab. 2013 Jun 4 17(6):976–987. https://doi.org/10.1016/j.cmet.2013.04.020
- Holmstrom KM, Pan X, Liu JC, et al. Assessment of cardiac function in mice lacking the mitochondrial calcium uniporter. J Mol Cell Cardiol. 2015 Aug;85:178–182.
- Luongo TS, Lambert JP, Yuan A, et al. The mitochondrial calcium uniporter matches energetic supply with cardiac workload during stress and modulates permeability transition. Cell Rep. 2015 Jul 7 12(1):23–34. https://doi.org/10.1016/j.celrep.2015.06.017
- Kwong JQ, Lu X, Correll RN, et al. The mitochondrial calcium uniporter selectively matches metabolic output to acute contractile stress in the heart. Cell Rep. 2015 Jul 7 12(1):15–22. https://doi.org/10.1016/j.celrep.2015.06.002
- Wu Y, Rasmussen TP, Koval OM, et al. The mitochondrial uniporter controls fight or flight heart rate increases. Nat Commun. 2015 Jan 20 6(1):6081. https://doi.org/10.1038/ncomms7081
- Rasmussen TP, Wu Y, Joiner ML, et al. Inhibition of MCU forces extramitochondrial adaptations governing physiological and pathological stress responses in heart. Proc Natl Acad Sci U S A. 2015 Jul 21 112(29):9129–9134. https://doi.org/10.1073/pnas.1504705112
- Kon N, Murakoshi M, Isobe A, et al. DS16570511 is a small-molecule inhibitor of the mitochondrial calcium uniporter. Cell Death Discov. 2017;3(1):17045. DOI:https://doi.org/10.1038/cddiscovery.2017.45.
- Bertero E, Nickel A, Kohlhaas M, et al. Loss of mitochondrial Ca(2+) uniporter limits inotropic reserve and provides trigger and substrate for arrhythmias in barth syndrome cardiomyopathy. Circulation. 2021 Nov 23 144(21):1694–1713. https://doi.org/10.1161/CIRCULATIONAHA.121.053755
- Suarez J, Cividini F, Scott BT, et al. Restoring mitochondrial calcium uniporter expression in diabetic mouse heart improves mitochondrial calcium handling and cardiac function. J Biol Chem. 2018 May 25 293(21):8182–8195. https://doi.org/10.1074/jbc.RA118.002066
- Lloyd-Evans E, Morgan AJ, He X, et al. Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium. Nat Med. 2008 Nov;14(11):1247–1255. DOI:https://doi.org/10.1038/nm.1876.
- Churchill GC, Okada Y, Thomas JM, et al. NAADP mobilizes Ca(2+) from reserve granules, lysosome-related organelles, in sea urchin eggs. Cell. 2002 Nov 27 111(5):703–708. https://doi.org/10.1016/S0092-8674(02)01082-6
- Luzio JP, Pryor PR, Bright NA. Lysosomes: fusion and function. Nat Rev Mol Cell Biol. 2007 Aug;8(8):622–632.
- Lopez-Sanjurjo CI, Tovey SC, Prole DL, et al. Lysosomes shape Ins(1,4,5)P3-evoked Ca2+ signals by selectively sequestering Ca2+ released from the endoplasmic reticulum. J Cell Sci. 2013 Jan 1 126(1):289–300. https://doi.org/10.1242/jcs.116103
- Morgan AJ, Davis LC, Wagner SK, et al. Bidirectional Ca(2)(+) signaling occurs between the endoplasmic reticulum and acidic organelles. J Cell Biol. 2013 Mar 18 200(6):789–805. https://doi.org/10.1083/jcb.201204078
- Christensen KA, Myers JT, Swanson JA. pH-dependent regulation of lysosomal calcium in macrophages. J Cell Sci. 2002 Feb 1; 115(Pt 3):599–607. https://doi.org/10.1242/jcs.115.3.599
- Morgan AJ, Platt FM, Lloyd-Evans E, et al. Molecular mechanisms of endolysosomal Ca2+ signalling in health and disease. Biochem J. 2011 Nov 1 439(3):349–374. https://doi.org/10.1042/BJ20110949
- Cheng X, Shen D, Samie M, et al. Mucolipins: intracellular TRPML1-3 channels. FEBS Lett. 2010 May 17 584(10):2013–2021. https://doi.org/10.1016/j.febslet.2009.12.056
- Chen Q, She J, Zeng W, et al. Structure of mammalian endolysosomal TRPML1 channel in nanodiscs. Nature. 2017 Oct 19 550(7676):415–418. https://doi.org/10.1038/nature24035
- Di Paola S, Scotto-Rosato A, Medina DL. TRPML1: the Ca((2+))retaker of the lysosome. Cell Calcium. 2018 Jan;69:112–121.
- Denis V, Cyert MS. Internal Ca(2+) release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue. J Cell Biol. 2002 Jan 7; 156(1):29–34. https://doi.org/10.1083/jcb.200111004
- Conn SJ, Gilliham M, Athman A, et al. Cell-specific vacuolar calcium storage mediated by CAX1 regulates apoplastic calcium concentration, gas exchange, and plant productivity in Arabidopsis. Plant Cell. 2011 Jan;23(1):240–257. DOI:https://doi.org/10.1105/tpc.109.072769.
- Cheng NH, Pittman JK, Shigaki T, et al. Functional association of Arabidopsis CAX1 and CAX3 is required for normal growth and ion homeostasis. Plant Physiol. 2005 Aug;138(4):2048–2060. DOI:https://doi.org/10.1104/pp.105.061218.
- Melchionda M, Pittman JK, Mayor R, et al. Ca2+/H+ exchange by acidic organelles regulates cell migration in vivo. J Cell Biol. 2016 Mar 28 212(7):803–813. https://doi.org/10.1083/jcb.201510019
- Saurav S, Tanwar J, Ahuja K, et al. Dysregulation of host cell calcium signaling during viral infections: emerging paradigm with high clinical relevance. Mol Aspects Med. 2021 Oct;81:101004.
- Moccia F, Negri S, Faris P, et al. Targeting endolysosomal two-pore channels to treat cardiovascular disorders in the Novel COronaVIrus disease 2019. Front Physiol. 2021;12:629119.
- Phillips MJ, Voeltz GK. Structure and function of ER membrane contact sites with other organelles. Nat Rev Mol Cell Biol. 2016 Feb;17(2):69–82.
- Yang J, Zhao Z, Gu M, et al. Release and uptake mechanisms of vesicular Ca(2+) stores. Protein Cell. 2019 Jan;10(1):8–19. DOI:https://doi.org/10.1007/s13238-018-0523-x.
- Xu H, Ren D. Lysosomal physiology. Annu Rev Physiol. 2015;77(1):57–80.
- Kumar S, Sanchez-Alvarez M, Lolo FN, et al. Autophagy and the lysosomal system in cancer. Cells. 2021 Oct 14 10(10):2752. https://doi.org/10.3390/cells10102752
- Grimm C, Butz E, Chen CC, et al. From mucolipidosis type IV to Ebola: TRPML and two-pore channels at the crossroads of endo-lysosomal trafficking and disease. Cell Calcium. 2017 Nov;67:148–155.
- Nair V, Belanger EC, Veinot JP. Lysosomal storage disorders affecting the heart: a review. Cardiovasc Pathol. 2019 Mar;39:12–24.
- Calcraft PJ, Ruas M, Pan Z, et al. NAADP mobilizes calcium from acidic organelles through two-pore channels. Nature. 2009 May 28 459(7246):596–600. https://doi.org/10.1038/nature08030
- Wang X, Zhang X, Dong XP, et al. TPC proteins are phosphoinositide- activated sodium-selective ion channels in endosomes and lysosomes. Cell. 2012 Oct 12 151(2):372–383. https://doi.org/10.1016/j.cell.2012.08.036
- Cang C, Zhou Y, Navarro B, et al. mTOR regulates lysosomal ATP-sensitive two-pore Na(+) channels to adapt to metabolic state. Cell. 2013 Feb 14 152(4):778–790. https://doi.org/10.1016/j.cell.2013.01.023
- Hooper R, Patel S. NAADP on target. Adv Exp Med Biol. 2012;740:325–347.
- Faris P, Pellavio G, Ferulli F, et al. Nicotinic Acid Adenine Dinucleotide Phosphate (NAADP) Induces Intracellular Ca(2+) Release through the Two-Pore Channel TPC1 in metastatic colorectal cancer cells. Cancers (Basel). 2019 Apr 15 11(4):542. https://doi.org/10.3390/cancers11040542
- Shen D, Wang X, Li X, et al. Lipid storage disorders block lysosomal trafficking by inhibiting a TRP channel and lysosomal calcium release. Nat Commun. 2012 Mar 13 3(1):731. https://doi.org/10.1038/ncomms1735
- Brailoiu E, Churamani D, Cai X, et al. Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling. J Cell Biol. 2009 Jul 27 186(2):201–209. https://doi.org/10.1083/jcb.200904073
- Terrar DA. Calcium Signaling in the Heart. Adv Exp Med Biol. 2020;1131:395–443.
- Patel S, Kilpatrick BS. Two-pore channels and disease. Biochim Biophys Acta Mol Cell Res. 2018 Nov;1865(11 Pt B):1678–1686.
- Gul R, Park DR, Shawl AI, et al. Nicotinic Acid Adenine Dinucleotide Phosphate (NAADP) and Cyclic ADP-Ribose (cADPR) Mediate Ca2+ Signaling in Cardiac Hypertrophy Induced by beta-Adrenergic Stimulation. PLoS One. 2016;11(3):e0149125. DOI:https://doi.org/10.1371/journal.pone.0149125.
- Zhang B, Watt JM, Cordiglieri C, et al. Small molecule antagonists of NAADP-Induced Ca(2+) Release in T-Lymphocytes suggest potential therapeutic agents for autoimmune disease. Sci Rep. [2018 Nov 13];8(1):16775.
- Zuo W, Liu N, Zeng Y, et al. CD38: a potential therapeutic target in cardiovascular disease. Cardiovasc Drugs Ther. 2021 Aug;35(4):815–828. DOI:https://doi.org/10.1007/s10557-020-07007-8.
- Sanchez M, Romero M, Gomez-Guzman M, et al. Cardiovascular effects of flavonoids. Curr Med Chem. 2019;26(39):6991–7034. DOI:https://doi.org/10.2174/0929867326666181220094721.
- Capel RA, Bolton EL, Lin WK, et al. Two-pore Channels (TPC2s) and Nicotinic Acid Adenine Dinucleotide Phosphate (NAADP) at lysosomal-sarcoplasmic reticular junctions contribute to acute and chronic beta-adrenoceptor signaling in the heart. J Biol Chem. 2015 Dec 11 290(50):30087–30098. https://doi.org/10.1074/jbc.M115.684076
- Jiang Y, Zhou Y, Peng G, et al. Two-pore channels mediated receptor-operated Ca(2+) entry in pulmonary artery smooth muscle cells in response to hypoxia. Int J Biochem Cell Biol. 2018 Apr;97:28–35.
- Davidson SM, Foote K, Kunuthur S, et al. Inhibition of NAADP signalling on reperfusion protects the heart by preventing lethal calcium oscillations via two-pore channel 1 and opening of the mitochondrial permeability transition pore. Cardiovasc Res. 2015 Dec 1 108(3):357–366. https://doi.org/10.1093/cvr/cvv226
- Ni L, Scott L Jr., Campbell HM, et al. Atrial-Specific Gene delivery using an adeno-associated viral vector. Circ Res. 2019 Jan 18;124(2):256–262. https://doi.org/10.1161/CIRCRESAHA.118.313811.
- Bilal AS, Blackwood EA, Thuerauf DJ, et al. Optimizing adeno-associated virus serotype 9 for studies of cardiac chamber-specific gene regulation. Circulation. 2021 May 18 143(20):2025–2027. https://doi.org/10.1161/CIRCULATIONAHA.120.052437
- Li H, Yang Y, Hong W, et al. Applications of genome editing technology in the targeted therapy of human diseases: mechanisms, advances and prospects. Signal Transduct Target Ther. 2020 Jan 3 5(1):1. https://doi.org/10.1038/s41392-019-0089-y
- Adli M. The CRISPR tool kit for genome editing and beyond. Nat Commun. 2018 May 15; 9(1):1911. https://doi.org/10.1038/s41467-018-04252-2
- Cannata A, Ali H, Sinagra G, et al. Gene therapy for the heart lessons learned and future perspectives. Circ Res. 2020 May 8 126(10):1394–1414. https://doi.org/10.1161/CIRCRESAHA.120.315855
- Li C, Samulski RJ. Engineering adeno-associated virus vectors for gene therapy. Nat Rev Genet. 2020 Apr;21(4):255–272.
- Chen AQ, Gao XF, Wang ZM, et al. Therapeutic exosomes in prognosis and developments of coronary artery disease. Front Cardiovasc Med. 2021;8:691548.
- Marshall WG Jr., Boone BA, Burgos JD, et al. Electroporation-mediated delivery of a naked DNA plasmid expressing VEGF to the porcine heart enhances protein expression. Gene Ther. 2010 Mar;17(3):419–423. DOI:https://doi.org/10.1038/gt.2009.153.
- Herweijer H, Wolff JA. Progress and prospects: naked DNA gene transfer and therapy. Gene Ther. 2003 Mar;10(6):453–458.
- Yan C, Quan XJ, Feng YM. Nanomedicine for gene delivery for the treatment of cardiovascular diseases. Curr Gene Ther. 2019;19(1):20–30.
- Mirza Z, Karim S. Nanoparticles-based drug delivery and gene therapy for breast cancer: recent advancements and future challenges. Semin Cancer Biol. 2021 Feb;69:226–237.0.