Structure and Function of the Bestrophin family of calcium-activated chloride channels

References

• Qu Z. The anion-selective pore of the bestrophins, a family of chloride channels associated with retinal degeneration. J Neurosci. 2006;26(20):5411–5419.
   PubMed Web of Science ®Google Scholar
• Qu Z, Cui Y, Hartzell C. A short motif in the C-terminus of mouse bestrophin 4 inhibits its activation as a Cl channel. FEBS Lett. 2006;580(8):2141–2146.
   PubMed Web of Science ®Google Scholar
• Qu Z, Fischmeister R, Hartzell C. Mouse Bestrophin-2 Is a Bona fide Cl− Channel. J Gen Physiol. 2004;123(4):327–340.
   PubMed Web of Science ®Google Scholar
• Qu Z, Hartzell C. Determinants of anion permeation in the second transmembrane domain of the mouse bestrophin-2 chloride channel. J Gen Physiol. 2004;124(4):371–382.
   PubMed Web of Science ®Google Scholar
• Qu Z, Hartzell HC. Bestrophin Cl − channels are highly permeable to HCO 3 −. Am J Physiol Cell Physiol. 2008;294(6):C1371–1377.
   PubMed Web of Science ®Google Scholar
• Qu ZQ, Yu K, Cui YY, et al. Activation of Bestrophin Cl– channels is regulated by C-terminal domains. J Biol Chem. 2007;282(24):17460–17467.
   PubMed Web of Science ®Google Scholar
• Sun H, Tsunenari T, Yau K-W, et al. The vitelliform macular dystrophy protein defines a new family of chloride channels. Proc Natl Acad Sci U S A. 2002;99(6):4008–4013.
   PubMed Web of Science ®Google Scholar
• Tsunenari T, Sun H, Williams J, et al. Structure-function analysis of the bestrophin family of anion channels. J Biol Chem. 2003;278(42):41114–41125.
   PubMed Web of Science ®Google Scholar
• Marquardt A. Mutations in a novel gene, VMD2, encoding a protein of unknown properties cause juvenile-onset vitelliform macular dystrophy (Best’s disease). Hum Mol Genet. 1998;7(9):1517–1525.
   PubMed Web of Science ®Google Scholar
• Petrukhin K, Koisti MJ, Bakall B, et al. Identification of the gene responsible for Best macular dystrophy. Nat Genet. 1998;19(3):241–247.
   PubMed Web of Science ®Google Scholar
• Blodi CF, Stone EM. Best’s vitelliform dystrophy. Ophthalmic Paediatr Genet. 1990;11(1):49–59.
   Google Scholar
• Boon CJ, Klevering BJ, Leroy BP, et al. The spectrum of ocular phenotypes caused by mutations in the BEST1 gene. Prog Retin Eye Res. 2009;28(3):187–205.
   PubMed Web of Science ®Google Scholar
• Marmorstein AD, Cross HE, Peachey NS. Functional roles of bestrophins in ocular epithelia. Prog Retin Eye Res. 2009;28(3):206–226.
   PubMed Web of Science ®Google Scholar
• Pasquay C, Wang LF, Lorenz B, et al. Bestrophin 1 – phenotypes and functional aspects in Bestrophinopathies. Ophthalmic Genet. 2015;36(3):193–212.
   PubMed Web of Science ®Google Scholar
• Kaufman SJ, Goldberg MF, Orth DH, et al. Autosomal dominant vitreoretinochoroidopathy. Arch Ophthalmol. 1982;100(2):272–278.
   PubMedGoogle Scholar
• Yardley J, Leroy BP, Hart-Holden N, et al. Mutations of VMD2 splicing regulators cause nanophthalmos and autosomal dominant Vitreoretinochoroidopathy (ADVIRC). Invest Ophthalmol Vis Sci. 2004;45(10):3683–3689.
   PubMed Web of Science ®Google Scholar
• Dalvin LA, Abou Chehade JE, Chiang J, et al. Retinitis pigmentosa associated with a mutation in BEST1. Am J Ophthalmol Case Rep. 2016;2:11–17.
   PubMedGoogle Scholar
• Davidson AE, Millar ID, Urquhart JE, et al. Missense mutations in a retinal pigment epithelium protein, bestrophin-1, cause retinitis pigmentosa. Am J Hum Genet. 2009;85(5):581–592.
   PubMed Web of Science ®Google Scholar
• Johnson AA, Guziewicz KE, Lee CJ, et al. Bestrophin 1 and retinal disease. Prog Retin Eye Res. 2017;58:45–69.
   PubMed Web of Science ®Google Scholar
• Xiao Q, Hartzell HC, Yu K. Bestrophins and retinopathies. Pflugers Arch. 2010;460(2):559–569.
   PubMed Web of Science ®Google Scholar
• Duran C, Thompson CH, Xiao Q, et al. Chloride channels: often enigmatic, rarely predictable. Annu Rev Physiol. 2010;72:95–121.
   PubMed Web of Science ®Google Scholar
• Hartzell C, Qu Z, Putzier I, et al. Looking chloride channels straight in the eye: bestrophins, lipofuscinosis, and retinal degeneration. Physiology (Bethesda). 2005;20:292–302.
   PubMed Web of Science ®Google Scholar
• Hartzell HC, Qu Z, Yu K, et al. Molecular physiology of bestrophins: multifunctional membrane proteins linked to best disease and other retinopathies. Physiol Rev. 2008;88(2):639–672.
   PubMed Web of Science ®Google Scholar
• Lehmann GL, Benedicto I, Philp NJ, et al. Plasma membrane protein polarity and trafficking in RPE cells: past, present and future. Exp Eye Res. 2014;126:5–15.
   PubMed Web of Science ®Google Scholar
• Stoops EH, Caplan MJ. Trafficking to the apical and basolateral membranes in polarized epithelial cells. J Am Soc Nephrol. 2014;25(7):1375–1386.
   PubMed Web of Science ®Google Scholar
• Zhao M, Chalmers L, Cao L, et al. Electrical signaling in control of ocular cell behaviors. Prog Retin Eye Res. 2012;31(1):65–88.
   PubMed Web of Science ®Google Scholar
• Bakall B, Marmorstein LY, Hoppe G, et al. Expression and localization of bestrophin during normal mouse development. Invest Ophthalmol Vis Sci. 2003;44(8):3622–3628.
   PubMed Web of Science ®Google Scholar
• Marmorstein AD, Kinnick TR, Stanton JB, et al. Bestrophin-1 influences transepithelial electrical properties and Ca2+ signaling in human retinal pigment epithelium. Mol Vis. 2015;21:347–359.
   PubMed Web of Science ®Google Scholar
• Marmorstein AD, Marmorstein LY, Rayborn M, et al. Bestrophin, the product of the Best vitelliform macular dystrophy gene (VMD2), localizes to the basolateral plasma membrane of the retinal pigment epithelium. Proc Natl Acad Sci U S A. 2000;97(23):12758–12763.
   PubMed Web of Science ®Google Scholar
• Mullins RF, Kuehn MH, Faidley EA, et al. Differential macular and peripheral expression of bestrophin in human eyes and its implication for best disease. Invest Ophthalmol Vis Sci. 2007;48(7):3372–3380.
   PubMed Web of Science ®Google Scholar
• Li Y, Zhang Y, Xu Y, et al. Patient-specific mutations impair BESTROPHIN1’s essential role in mediating Ca(2+)-dependent Cl(-) currents in human RPE. Elife. 2017;6. DOI:https://doi.org/10.7554/eLife.29914.
   Google Scholar
• Cordes M, Bucichowski P, Alfaar AS, et al. Inhibition of Ca(2+) channel surface expression by mutant bestrophin-1 in RPE cells. FASEB J. 2020;34(3):4055–4071.
   PubMed Web of Science ®Google Scholar
• Marmorstein LY, Wu J, McLaughlin P, et al. The light peak of the electroretinogram is dependent on voltage-gated calcium channels and antagonized by bestrophin (best-1). J Gen Physiol. 2006;127(5):577–589.
   PubMed Web of Science ®Google Scholar
• Milenkovic A, Brandl C, Milenkovic VM, et al. Bestrophin 1 is indispensable for volume regulation in human retinal pigment epithelium cells. Proc Natl Acad Sci U S A. 2015;112(20):E2630–2639.
   PubMed Web of Science ®Google Scholar
• Wu J, Marmorstein AD, Striessnig J, et al. Voltage-dependent calcium channel Ca V 1.3 subunits regulate the light peak of the electroretinogram. J Neurophysiol. 2007;97(5):3731–3735.
   PubMed Web of Science ®Google Scholar
• Yu K, Xiao Q, Cui G, et al. The best disease-linked Cl- channel hBest1 regulates CaV1 (L-type) Ca2+ channels via src-homology-binding domains. J Neurosci. 2008;28(22):5660–5670.
   PubMed Web of Science ®Google Scholar
• Aldehni F, Spitzner M, Martins JR, et al. Bestrophin 1 promotes epithelial-to-mesenchymal transition of renal collecting duct cells. J Am Soc Nephrol. 2009;20(7):1556–1564.
   PubMed Web of Science ®Google Scholar
• Barro Soria R, Spitzner M, Schreiber R, et al. Bestrophin-1 enables Ca2+-activated Cl- conductance in epithelia. J Biol Chem. 2009;284(43):29405–29412.
   PubMed Web of Science ®Google Scholar
• Barro-Soria R, Schreiber R, Kunzelmann K. Bestrophin 1 and 2 are components of the Ca(2+) activated Cl(-) conductance in mouse airways. Biochim Biophys Acta. 2008;1783(10):1993–2000.
   PubMed Web of Science ®Google Scholar
• Boudes M, Sar C, Menigoz A, et al. Best1 is a gene regulated by nerve injury and required for Ca2+-activated Cl- current expression in axotomized sensory neurons. J Neurosci. 2009;29(32):10063–10071.
   PubMed Web of Science ®Google Scholar
• Lee S, Yoon BE, Berglund K, et al. Channel-mediated tonic GABA release from glia. Science. 2010;330(6005):790–796.
   PubMed Web of Science ®Google Scholar
• Marsey LL, Winpenny JP. Bestrophin expression and function in the human pancreatic duct cell line, CFPAC-1. J Physiol. 2009;587(10):2211–2224.
   PubMed Web of Science ®Google Scholar
• Oh S-J, Lee CJ. Distribution and Function of the Bestrophin-1 (Best1) channel in the brain. Exp Neurobiol. 2017;26(3):113–121.
   PubMed Web of Science ®Google Scholar
• Spitzner M, Martins JR, Soria RB, et al. Eag1 and Bestrophin 1 are up-regulated in fast-growing colonic cancer cells. J Biol Chem. 2008;283(12):7421–7428.
   PubMed Web of Science ®Google Scholar
• Kramer F, Stohr H, Weber BH. Cloning and characterization of the murine Vmd2 RFP-TM gene family. Cytogenet Genome Res. 2004;105(1):107–114.
   PubMed Web of Science ®Google Scholar
• Stohr H, Marquardt A, Nanda I, et al. Three novel human VMD2-like genes are members of the evolutionary highly conserved RFP-TM family. Eur J Hum Genet. 2002;10(4):281–284.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Patil RV, Marmorstein AD. Bestrophin 2 is expressed in human non-pigmented ciliary epithelium but not retinal pigment epithelium. Mol Vis. 2010;16:200–206.
   PubMed Web of Science ®Google Scholar
• Delamere NA. Ciliary Body and Ciliary Epithelium. Adv Organ Biol. 2005;10:127–148.
   PubMedGoogle Scholar
• Bakall B, McLaughlin P, Stanton JB, et al. Bestrophin-2 is involved in the generation of intraocular pressure. Invest Ophthalmol Vis Sci. 2008;49(4):1563–1570.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Davidson BR, Stamer WD, et al. Enhanced inflow and outflow rates despite lower IOP in bestrophin-2-deficient mice. Invest Ophthalmol Vis Sci. 2009;50(2):765–770.
   PubMed Web of Science ®Google Scholar
• Cui CY, Childress V, Piao Y, et al. Forkhead transcription factor FoxA1 regulates sweat secretion through Bestrophin 2 anion channel and Na-K-Cl cotransporter 1. Proc Natl Acad Sci U S A. 2012;109(4):1199–1203.
   PubMed Web of Science ®Google Scholar
• Klimmeck D, Daiber PC, Brühl A, et al. Bestrophin 2: an anion channel associated with neurogenesis in chemosensory systems. J Comp Neurol. 2009;515(5):585–599.
   PubMed Web of Science ®Google Scholar
• Pifferi S, Dibattista M, Sagheddu C, et al. Calcium-activated chloride currents in olfactory sensory neurons from mice lacking bestrophin-2. J Physiol. 2009;587(17):4265–4279.
   PubMed Web of Science ®Google Scholar
• Pifferi S, Pascarella G, Boccaccio A, et al. Bestrophin-2 is a candidate calcium-activated chloride channel involved in olfactory transduction. Proc Natl Acad Sci U S A. 2006;103(34):12929–12934.
   PubMed Web of Science ®Google Scholar
• Yu K, Lujan R, Marmorstein A, et al. Bestrophin-2 mediates bicarbonate transport by goblet cells in mouse colon. J Clin Invest. 2010;120(5):1722–1735.
   PubMed Web of Science ®Google Scholar
• Hegyi B, Horvath B, Vaczi K, et al. Ca(2+)-activated Cl(-) current is antiarrhythmic by reducing both spatial and temporal heterogeneity of cardiac repolarization. J Mol Cell Cardiol. 2017;109:27–37.
   PubMed Web of Science ®Google Scholar
• Broegger T, Jacobsen JC, Secher Dam V, et al. Bestrophin is important for the rhythmic but not the tonic contraction in rat mesenteric small arteries. Cardiovasc Res. 2011;91(4):685–693.
   PubMed Web of Science ®Google Scholar
• Dam VS, Boedtkjer DM, Aalkjaer C, et al. The bestrophin- and TMEM16A-associated Ca(2+)- activated Cl(-) channels in vascular smooth muscles. Channels (Austin). 2014;8(4):361–369.
   PubMed Web of Science ®Google Scholar
• Matchkov VV, Larsen P, Bouzinova EV, et al. Bestrophin-3 (Vitelliform Macular Dystrophy 2–Like 3 Protein) is essential for the cGMP-dependent calcium-activated chloride conductance in vascular smooth muscle cells. Circ Res. 2008;103(8):864–872.
   PubMed Web of Science ®Google Scholar
• O’Driscoll KE, Hatton WJ, Burkin HR, et al. Expression, localization, and functional properties of Bestrophin 3 channel isolated from mouse heart. Am J Physiol Cell Physiol. 2008;295(6):C1610–1624.
   PubMed Web of Science ®Google Scholar
• Golubinskaya V, Elvin J, Ebefors K, et al. Bestrophin-3 is differently expressed in normal and injured mouse glomerular podocytes. Acta Physiol (Oxf). 2015;214(4):481–496.
   PubMed Web of Science ®Google Scholar
• Golubinskaya V, Vontell R, Supramaniam V, et al. Bestrophin-3 Expression in a Subpopulation of Astrocytes in the Neonatal Brain After Hypoxic-Ischemic Injury. Front Physiol. 2019;10:23.
   PubMed Web of Science ®Google Scholar
• Lee WK, Chakraborty PK, Roussa E, et al. ERK1/2-dependent bestrophin-3 expression prevents ER-stress-induced cell death in renal epithelial cells by reducing CHOP. Biochim Biophys Acta. 2012;1823(10):1864–1876.
   PubMed Web of Science ®Google Scholar
• Ito G, Okamoto R, Murano T, et al. Lineage-specific expression of bestrophin-2 and bestrophin-4 in human intestinal epithelial cells. PLoS One. 2013;8(11):e79693.
   PubMed Web of Science ®Google Scholar
• Milenkovic VM, Langmann T, Schreiber R, et al. Molecular evolution and functional divergence of the bestrophin protein family. BMC Evol Biol. 2008;8(1):72.
   PubMed Web of Science ®Google Scholar
• Hagen AR, Barabote RD, Saier MH. The bestrophin family of anion channels: identification of prokaryotic homologues. Mol Membr Biol. 2005;22(4):291–302.
   PubMed Web of Science ®Google Scholar
• Eisenman G, Horn R. Ionic selectivity revisited: the role of kinetic and equilibrium processes in ion permeation through channels. J Membr Biol. 1983;76(3):197–225.
   PubMed Web of Science ®Google Scholar
• Wright EM, Diamond JM. Anion selectivity in biological systems. Physiol Rev. 1977;57(1):109–156.
   PubMed Web of Science ®Google Scholar
• Duta V, Szkotak AJ, Nahirney D, et al. The role of bestrophin in airway epithelial ion transport. FEBS Lett. 2004;577(3):551–554.
   PubMed Web of Science ®Google Scholar
• Liu Y, Zhang H, Huang D, et al. Characterization of the effects of Cl(-) channel modulators on TMEM16A and bestrophin-1 Ca(2)(+) activated Cl(-) channels. Pflugers Arch. 2015;467(7):1417–1430.
   PubMed Web of Science ®Google Scholar
• O’Driscoll KE, Leblanc N, Hatton WJ, et al. Functional properties of murine bestrophin 1 channel. Biochem Biophys Res Commun. 2009;384(4):476–481.
   PubMed Web of Science ®Google Scholar
• Yang T, Liu Q, Kloss B, et al. Structure and selectivity in bestrophin ion channels. Science. 2014;346(6207):355–359.
   PubMed Web of Science ®Google Scholar
• Bruni R, Kloss B. High-throughput cloning and expression of integral membrane proteins in Escherichia coli. Curr Protoc Protein Sci. 2013;74. DOI:https://doi.org/10.1002/0471140864.ps2906s74. 29 26 21-29 26 34
   Google Scholar
• Kane Dickson V, Pedi L, Long SB. Structure and insights into the function of a Ca(2+)-activated Cl(-) channel. Nature. 2014;516(7530):213–218.
   PubMed Web of Science ®Google Scholar
• Ji C, Kittredge A, Hopiavuori A, et al. Dual Ca(2+)-dependent gates in human Bestrophin1 underlie disease-causing mechanisms of gain-of-function mutations. Commun Biol. 2019;2:240.
   PubMed Web of Science ®Google Scholar
• Miller AN, Vaisey G, Long SB. 2019. Molecular mechanisms of gating in the calcium-activated chloride channel bestrophin. Elife;8. https://doi.org/10.7554/eLife.43231
   Google Scholar
• Vaisey G, Long SB. An allosteric mechanism of inactivation in the calcium-dependent chloride channel BEST1. J Gen Physiol. 2018;150(11):1484–1497.
   PubMed Web of Science ®Google Scholar
• Vaisey G, Miller AN, Long SB. Distinct regions that control ion selectivity and calcium-dependent activation in the bestrophin ion channel. Proc Natl Acad Sci U S A. 2016;113(47):E7399–e7408.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Kittredge A, Ward N, et al. ATP activates bestrophin ion channels through direct interaction. Nat Commun. 2018;9(1):3126.
   PubMed Web of Science ®Google Scholar
• Kittredge A, Ward N, Hopiavuori A, et al. Expression and purification of Mammalian Bestrophin ion channels. J Vis Exp. 2018;(138). DOI:https://doi.org/10.3791/57832.
   Google Scholar
• Owji AP, Zhao Q, Ji C, et al. Structural and functional characterization of the bestrophin-2 anion channel. Nat Struct Mol Biol. 2020;27(4):382–391.
   PubMed Web of Science ®Google Scholar
• Chien LT, Zhang ZR, Hartzell HC. Single Cl- channels activated by Ca2+ in Drosophila S2 cells are mediated by bestrophins. J Gen Physiol. 2006;128(3):247–259.
   PubMed Web of Science ®Google Scholar
• Rao S, Klesse G, Stansfeld PJ, et al. A BEST example of channel structure annotation by molecular simulation. Channels (Austin). 2017;11(4):347–353.
   PubMed Web of Science ®Google Scholar
• Xiao Q, Yu K, Cui -Y-Y, et al. Dysregulation of human bestrophin-1 by ceramide-induced dephosphorylation. J Physiol. 2009;587(18):4379–4391.
   PubMed Web of Science ®Google Scholar
• Csanady L, Vergani P, Gadsby DC. Structure, gating, and regulation of the Cftr anion channel. Physiol Rev. 2019;99(1):707–738.
   PubMed Web of Science ®Google Scholar
• Schreiber M, Salkoff L. A novel calcium-sensing domain in the BK channel. Biophys J. 1997;73(3):1355–1363.
   PubMed Web of Science ®Google Scholar
• Tsunenari T, Nathans J, Yau K-W. Ca2+-activated Cl− Current from human bestrophin-4 in excised membrane patches. J Gen Physiol. 2006;127(6):749–754.
   PubMed Web of Science ®Google Scholar
• Xiao Q, Prussia A, Yu K, et al. Regulation of bestrophin Cl channels by calcium: role of the C terminus. J Gen Physiol. 2008;132(6):681–692.
   PubMed Web of Science ®Google Scholar
• Bitner H, Schatz P, Mizrahi-Meissonnier L, et al. Frequency, genotype, and clinical spectrum of best vitelliform macular dystrophy: data from a national center in Denmark. Am J Ophthalmol. 2012;154(2):403–412.e404.
   PubMed Web of Science ®Google Scholar
• Frecer V, Iarossi G, Salvetti AP, et al. Pathogenicity of new BEST1 variants identified in Italian patients with best vitelliform macular dystrophy assessed by computational structural biology. J Transl Med. 2019;17(1):330.
   PubMed Web of Science ®Google Scholar
• Kranjc A, Grillo FW, Rievaj J, et al. Regulation of bestrophins by Ca2+: a theoretical and experimental study. PLoS One. 2009;4(3):e4672.
   PubMed Web of Science ®Google Scholar
• Lin Y, Li T, Ma C, et al. Genetic variations in Bestrophin‑1 and associated clinical findings in two Chinese patients with juvenile‑onset and adult‑onset best vitelliform macular dystrophy. Mol Med Rep. 2018;17(1):225–233.
   PubMed Web of Science ®Google Scholar
• Marchant D, Yu K, Bigot K, et al. New VMD2 gene mutations identified in patients affected by Best vitelliform macular dystrophy. J Med Genet. 2007;44(3):e70.
   PubMed Web of Science ®Google Scholar
• Tian R, Yang G, Wang J, et al. Screening for BEST1 gene mutations in Chinese patients with bestrophinopathy. Mol Vis. 2014;20:1594–1604.
   PubMed Web of Science ®Google Scholar
• Marmorstein LY, McLaughlin PJ, Stanton JB, et al. Bestrophin interacts physically and functionally with protein phosphatase 2A. J Biol Chem. 2002;277(34):30591–30597.
   PubMed Web of Science ®Google Scholar
• Oh S-J, Woo J, Lee Y-S, et al. Direct interaction with 14–3-3γ promotes surface expression of Best1 channel in astrocyte. Mol Brain. 2017;10(1):51.
   PubMed Web of Science ®Google Scholar
• Duran C, Chien LT, Hartzell HC. Drosophila bestrophin-1 currents are regulated by phosphorylation via a CaMKII dependent mechanism. PLoS One. 2013;8(3):e58875.
   PubMed Web of Science ®Google Scholar
• Yang T, Justus S, Li Y, et al. BEST1: the best target for gene and cell therapies. Mol Ther. 2015;23(12):1805–1809.
   PubMed Web of Science ®Google Scholar
• Qu Z, Wei RW, Mann W, et al. Two Bestrophins cloned from xenopus laevis oocytes express Ca2+-activated Cl- currents. J Biol Chem. 2003;278(49):49563–49572.
   PubMed Web of Science ®Google Scholar
• Idelson M, Alper R, Obolensky A, et al. Directed differentiation of human embryonic stem cells into functional retinal pigment epithelium cells. Cell Stem Cell. 2009;5(4):396–408.
   PubMed Web of Science ®Google Scholar
• Kittredge A, Ji C, Zhang Y, et al. Differentiation, maintenance, and analysis of human retinal pigment epithelium cells: a disease-in-a-dish model for Best1 mutations. J Vis Exp. 2018;(138). DOI:https://doi.org/10.3791/57791.
   Google Scholar
• Kittredge A, Zhang Y, Yang T. Evaluating BEST1 mutations in pluripotent stem cell-derived retinal pigment epithelial cells. Methods Enzymol. 2021;654:365–382.
   PubMed Web of Science ®Google Scholar
• Maminishkis A, Chen S, Jalickee S, et al. Confluent monolayers of cultured human fetal retinal pigment epithelium exhibit morphology and physiology of native tissue. Invest Ophthalmol Vis Sci. 2006;47(8):3612–3624.
   PubMed Web of Science ®Google Scholar
• Maruotti J, Wahlin K, Gorrell D, et al. A simple and scalable process for the differentiation of retinal pigment epithelium from human pluripotent stem cells. Stem Cells Transl Med. 2013;2(5):341–354.
   PubMed Web of Science ®Google Scholar
• Meyer JS, Howden SE, Wallace KA, et al. Optic vesicle-like structures derived from human pluripotent stem cells facilitate a customized approach to retinal disease treatment. Stem Cells. 2011;29(8):1206–1218.
   PubMed Web of Science ®Google Scholar
• Meyer JS, Shearer RL, Capowski EE, et al. Modeling early retinal development with human embryonic and induced pluripotent stem cells. Proc Natl Acad Sci U S A. 2009;106(39):16698–16703.
   PubMed Web of Science ®Google Scholar
• Phillips MJ, Wallace KA, Dickerson SJ, et al. Blood-derived human iPS cells generate optic vesicle–like structures with the capacity to form retinal laminae and develop synapses. Invest Ophthalmol Vis Sci. 2012;53(4):2007–2019.
   PubMed Web of Science ®Google Scholar
• Lee JH, Oh JO, Lee CS. Induced pluripotent stem cell modeling of best disease and autosomal recessive Bestrophinopathy. Yonsei Med J. 2020;61(9):816–825.
   PubMed Web of Science ®Google Scholar
• Lin TC, Lin YY, Hsu CC, et al. Nanomedicine-based curcumin approach improved ROS damage in best dystrophy-specific induced pluripotent stem cells. Cell Transplant. 2019;28(11):1345–1357.
   PubMed Web of Science ®Google Scholar
• Marmorstein AD, Johnson AA, Bachman LA, et al. Mutant Best1 expression and impaired phagocytosis in an iPSC model of autosomal recessive Bestrophinopathy. Sci Rep. 2018;8(1):4487.
   PubMed Web of Science ®Google Scholar
• Moshfegh Y, Velez G, Li Y, et al. BESTROPHIN1 mutations cause defective chloride conductance in patient stem cell-derived RPE. Hum Mol Genet. 2016;25(13):2672–2680.
   PubMed Web of Science ®Google Scholar
• Nachtigal A-L, Milenkovic A, Brandl C, et al. Mutation-dependent pathomechanisms determine the phenotype in the Bestrophinopathies. Int J Mol Sci. 2020;21(5):1597.
   Web of Science ®Google Scholar
• Singh R, Kuai D, Guziewicz KE, et al. Pharmacological modulation of photoreceptor outer segment degradation in a human iPS cell model of inherited macular degeneration. Mol Ther. 2015;23(11):1700–1711.
   PubMed Web of Science ®Google Scholar
• Singh R, Shen W, Kuai D, et al. iPS cell modeling of Best disease: insights into the pathophysiology of an inherited macular degeneration. Hum Mol Genet. 2013;22(3):593–607.
   PubMed Web of Science ®Google Scholar
• Liu J, Taylor RL, Baines RA, et al. Small molecules restore Bestrophin 1 expression and function of both dominant and recessive Bestrophinopathies in patient-derived retinal pigment epithelium. Invest Ophthalmol Vis Sci. 2020;61(5):28.
   PubMed Web of Science ®Google Scholar
• Sinha D, Steyer B, Shahi PK, et al. Human iPSC modeling reveals mutation-specific responses to gene therapy in a genotypically diverse dominant maculopathy. Am J Hum Genet. 2020;107(2):278–292.
   PubMed Web of Science ®Google Scholar
• Ji C, Li Y, Kittredge A, et al. Investigation and restoration of BEST1 activity in patient-derived RPEs with dominant mutations. Sci Rep. 2019;9(1):19026.
   PubMed Web of Science ®Google Scholar
• Zhao Q, Kong Y, Kittredge A, et al. Distinct expression requirements and rescue strategies for BEST1 loss- and gain-of-function mutations. Elife. 2021;10. DOI:https://doi.org/10.7554/eLife.67622.
   Google Scholar
• Guziewicz KE, Cideciyan AV, Beltran WA, et al. BEST1 gene therapy corrects a diffuse retina-wide microdetachment modulated by light exposure. Proc Natl Acad Sci U S A. 2018;115(12):E2839–E2848.
   PubMed Web of Science ®Google Scholar
• Wang Y, Tang Z, Gu P. Stem/progenitor cell-based transplantation for retinal degeneration: a review of clinical trials. Cell Death Dis. 2020;11(9):793.
   PubMed Web of Science ®Google Scholar