Dysregulated Inflammatory Signaling upon Charcot-Marie-Tooth Type 1C Mutation of SIMPLE Protein

REFERENCES

• Magalhaes AC, Dunn H, Ferguson SS. 2011. Regulation of G protein-coupled receptor activity, trafficking, and localization by Gpcr-interacting proteins. Br J Pharmacol 165:1717–1736. http://dx.doi.org/10.1111/j.1476-5381.2011.01552.x.
   Google Scholar
• Marchese A, Paing MM, Temple BR, Trejo J. 2008. G protein-coupled receptor sorting to endosomes and lysosomes. Annu Rev Pharmacol Toxicol 48:601–629. http://dx.doi.org/10.1146/annurev.pharmtox.48.113006.094646.
   PubMed Web of Science ®Google Scholar
• Platta HW, Stenmark H. 2011. Endocytosis and signaling. Curr Opin Cell Biol 23:393–403. http://dx.doi.org/10.1016/j.ceb.2011.03.008.
   PubMed Web of Science ®Google Scholar
• Sorkin A, Goh LK. 2009. Endocytosis and intracellular trafficking of ErbBs. Exp Cell Res 315:683–696. http://dx.doi.org/10.1016/j.yexcr.2008.07.029.
   PubMed Web of Science ®Google Scholar
• Zwang Y, Yarden Y. 2009. Systems biology of growth factor-induced receptor endocytosis. Traffic 10:349–363. http://dx.doi.org/10.1111/j.1600-0854.2008.00870.x.
   PubMedGoogle Scholar
• Katoh Y, Shiba Y, Mitsuhashi H, Yanagida Y, Takatsu H, Nakayama K. 2004. Tollip and Tom1 form a complex and recruit ubiquitin-conjugated proteins onto early endosomes. J Biol Chem 279:24435–24443. http://dx.doi.org/10.1074/jbc.M400059200.
   PubMedGoogle Scholar
• Premont RT, Gainetdinov RR. 2007. Physiological roles of G protein-coupled receptor kinases and arrestins. Annu Rev Physiol 69:511–534. http://dx.doi.org/10.1146/annurev.physiol.69.022405.154731.
   PubMed Web of Science ®Google Scholar
• Wang T, Liu NS, Seet LF, Hong W. 2010. The emerging role of VHS domain-containing Tom1, Tom1L1, and Tom1L2 in membrane trafficking. Traffic 11:1119–1128. http://dx.doi.org/10.1111/j.1600-0854.2010.01098.x.
   PubMedGoogle Scholar
• Babst M. 2011. MVB vesicle formation: ESCRT-dependent, ESCRT-independent, and everything in between. Curr Opin Cell Biol 23:452–457. http://dx.doi.org/10.1016/j.ceb.2011.04.008.
   PubMed Web of Science ®Google Scholar
• Henne WM, Buchkovich NJ, Emr SD. 2011. The ESCRT pathway. Dev Cell 21:77–91. http://dx.doi.org/10.1016/j.devcel.2011.05.015.
   PubMed Web of Science ®Google Scholar
• Hurley JH. 2010. The ESCRT complexes. Crit Rev Biochem Mol Biol 45:463–487. http://dx.doi.org/10.3109/10409238.2010.502516.
   PubMed Web of Science ®Google Scholar
• Rusten TE, Vaccari T, Stenmark H. 2012. Shaping development with ESCRTs. Nat Cell Biol 14:38–45. http://dx.doi.org/10.1038/nrm3495.
   PubMed Web of Science ®Google Scholar
• Keller S, Sanderson MP, Stoeck A, Altevogt P. 2006. Exosomes: from biogenesis and secretion to biological function. Immunol Lett 107:102–108. http://dx.doi.org/10.1016/j.imlet.2006.09.005.
   PubMed Web of Science ®Google Scholar
• van Niel G, Porto-Carreiro I, Simoes S, Raposo G. 2006. Exosomes: a common pathway for a specialized function. J Biochem 140:13–21. http://dx.doi.org/10.1093/jb/mvj128.
   PubMed Web of Science ®Google Scholar
• Vella LJ, Sharples RA, Nisbet RM, Cappai R, Hill AF. 2008. The role of exosomes in the processing of proteins associated with neurodegenerative diseases. Eur Biophysics J 37:323–332. http://dx.doi.org/10.1007/s00249-007-0246-z.
   PubMed Web of Science ®Google Scholar
• Brankatschk B, Wichert SP, Johnson SD, Schaad O, Rossner MJ, Gruenberg J. 2012. Regulation of the EGF transcriptional response by endocytic sorting. Sci Signal 5:ra21. http://dx.doi.org/10.1126/scisignal.2002351.
   PubMedGoogle Scholar
• Falguières T, Luyet P-P, Gruenberg J. 2009. Molecular assemblies and membrane domains in multivesicular endosome dynamics. Exp Cell Res 315:1567–1573. http://dx.doi.org/10.1016/j.yexcr.2008.12.006.
   PubMed Web of Science ®Google Scholar
• Lobert VH, Stenmark H. 2011. Cell polarity and migration: emerging role for the endosomal sorting machinery. Physiology (Bethesda) 26:171–180. http://dx.doi.org/10.1152/physiol.00054.2010.
   PubMedGoogle Scholar
• Saksena S, Emr SD. 2009. ESCRTs and human disease. Biochem Soc Trans 037:167–172. http://dx.doi.org/10.1042/BST0370167.
   Google Scholar
• Stuffers S, Brech A, Stenmark H. 2009. ESCRT proteins in physiology and disease. Exp Cell Res 315:1619–1626. http://dx.doi.org/10.1016/j.yexcr.2008.10.013.
   PubMedGoogle Scholar
• Gasparrini F, Molfetta R, Quatrini L, Frati L, Santoni A, Paolini R. 2012. Syk-dependent regulation of Hrs phosphorylation and ubiquitination upon FεRI engagement: impact on Hrs membrane/cytosol localization. Eur J Immunol 42:2744–2753. http://dx.doi.org/10.1002/eji.201142278.
   PubMedGoogle Scholar
• Row PE, Clague MJ, Urbe S. 2005. Growth factors induce differential phosphorylation profiles of the Hrs-STAM complex: a common node in signaling networks with signal-specific properties. Biochem J 389:629–636. http://dx.doi.org/10.1042/BJ20050067.
   PubMedGoogle Scholar
• Stern KA, Visser Smit GD, Place TL, Winistorfer S, Piper RC, Lill NL. 2007. Epidermal growth factor receptor fate is controlled by Hrs tyrosine phosphorylation sites that regulate Hrs degradation. Mol Cell Biol 27:888–898. http://dx.doi.org/10.1128/MCB.02356-05.
   PubMedGoogle Scholar
• Zhu H, Guariglia S, Yu RY, Li W, Brancho D, Peinado H, Lyden D, Salzer J, Bennett C, Chow CW. 2013. Mutation of SIMPLE in Charcot-Marie-Tooth 1C alters production of exosomes. Mol Biol Cell 24:1619–1637. http://dx.doi.org/10.1091/mbc.E12-07-0544.
   PubMed Web of Science ®Google Scholar
• Bennett CL, Shirk AJ, Huynh HM, Street VA, Nelis E, Van Maldergem L, De Jonghe P, Jordanova A, Guergueltcheva V, Tournev I, Van Den Bergh P, Seeman P, Mazanec R, Prochazka T, Kremensky I, Haberlova J, Weiss MD, Timmerman V, Bird TD, Chance PF. 2004. SIMPLE mutation in demyelinating neuropathy and distribution in sciatic nerve. Ann Neurol 55:713–720. http://dx.doi.org/10.1002/ana.20094.
   PubMedGoogle Scholar
• Gerding WM, Koetting J, Epplen JT, Neusch C. 2009. Hereditary motor and sensory neuropathy caused by a novel mutation in LITAF. Neuromuscular Disorders 19:701–703. http://dx.doi.org/10.1016/j.nmd.2009.05.006.
   PubMed Web of Science ®Google Scholar
• Latour P, Gonnaud PM, Ollagnon E, Chan V, Perelman S, Stojkovic T, Stoll C, Vial C, Ziegler F, Vandenberghe A, Maire I. 2006. SIMPLE mutation analysis in dominant demyelinating Charcot-Marie-Tooth disease: three novel mutations. J Peripher Nerv Syst 11:148–155. http://dx.doi.org/10.1111/j.1085-9489.2006.00080.x.
   PubMed Web of Science ®Google Scholar
• Saifi GM, Szigeti K, Wiszniewski W, Shy ME, Krajewski K, Hausmanowa-Petrusewicz I, Kochanski A, Reeser S, Mancias P, Butler I, Lupski JR. 2005. SIMPLE mutations in Charcot-Marie-Tooth disease and the potential role of its protein product in protein degradation. Hum Mutat 25:372–383. http://dx.doi.org/10.1002/humu.20153.
   PubMedGoogle Scholar
• Street VA, Goldy JD, Golden AS, Tempel BL, Bird TD, Chance PF. 2002. Mapping of Charcot-Marie-Tooth disease type 1C to chromosome 16p identifies a novel locus for demyelinating neuropathies. Am J Hum Genet 70:244–250. http://dx.doi.org/10.1086/337943.
   PubMedGoogle Scholar
• Somandin C, Gerber D, Pereira JA, Horn M, Suter U. 2012. LITAF (SIMPLE) regulates Wallerian degeneration after injury but is not essential for peripheral nerve development and maintenance: implications for Charcot-Marie-Tooth disease. Glia 60:1518–1528. http://dx.doi.org/10.1002/glia.22371.
   PubMedGoogle Scholar
• Qian B, Deng Y, Im JH, Muschel RJ, Zou Y, Li J, Lang RA, Pollard JW. 2009. A distinct macrophage population mediates metastatic breast cancer cell extravasation, establishment, and growth. PLoS One 4:e6562. http://dx.doi.org/10.1371/journal.pone.0006562.
   PubMed Web of Science ®Google Scholar
• Yang TT, Suk HY, Yang X, Olabisi O, Yu RY, Durand J, Jelicks LA, Kim JY, Scherer PE, Wang Y, Feng Y, Rossetti L, Graef IA, Crabtree GR, Chow CW. 2006. Role of transcription factor NFAT in glucose and insulin homeostasis. Mol Cell Biol 26:7372–7387. http://dx.doi.org/10.1128/MCB.00580-06.
   PubMedGoogle Scholar
• Yang DP, Kim J, Syed N, Tung YJ, Bhaskaran A, Mindos T, Mirsky R, Jessen KR, Maurel P, Parkinson DB, Kim HA. 2012. p38 MAPK activation promotes denervated Schwann cell phenotype and functions as a negative regulator of Schwann cell differentiation and myelination. J Neurosci 32:7158–7168. http://dx.doi.org/10.1523/JNEUROSCI.5812-11.2012.
   PubMed Web of Science ®Google Scholar
• Shirk AJ, Anderson SK, Hashemi SH, Chance PF, Bennett CL. 2005. SIMPLE interacts with NEDD4 and TSG101: evidence for a role in lysosomal sorting and implications for Charcot-Marie-Tooth disease. J Neurosci Res 82:43–50. http://dx.doi.org/10.1002/jnr.20628.
   PubMedGoogle Scholar
• Bache KG, Brech A, Mehlum A, Stenmark H. 2003. Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J Cell Biol 162:435–442. http://dx.doi.org/10.1083/jcb.200302131.
   PubMed Web of Science ®Google Scholar
• Razi M, Futter CE. 2006. Distinct roles for Tsg101 and Hrs in multivesicular body formation and inward vesiculation. Mol Biol Cell 17:3469–3483. http://dx.doi.org/10.1091/mbc.E05-11-1054.
   PubMed Web of Science ®Google Scholar
• Eaton HE, Desrochers G, Drory SB, Metcalf J, Angers A, Brunetti CR. 2011. SIMPLE/LITAF expression induces the translocation of the ubiquitin ligase itch towards the lysosomal compartments. PLoS One 6:e16873. http://dx.doi.org/10.1371/journal.pone.0016873.
   PubMedGoogle Scholar
• Chen YG. 2009. Endocytic regulation of TGF-beta signaling. Cell Res 19:58–70. http://dx.doi.org/10.1038/cr.2008.315.
   PubMed Web of Science ®Google Scholar
• De Boeck M, ten Dijke P. 2012. Key role for ubiquitin protein modification in TGFβ signal transduction. Uppsala J Med Sci 117:153–165. http://dx.doi.org/10.3109/03009734.2012.654858.
   PubMed Web of Science ®Google Scholar
• Heldin CH, Landstrom M, Moustakas A. 2009. Mechanism of TGF-β signaling to growth arrest, apoptosis, and epithelial-mesenchymal transition. Curr Opin Cell Biol 21:166–176. http://dx.doi.org/10.1016/j.ceb.2009.01.021.
   PubMed Web of Science ®Google Scholar
• Mu Y, Gudey SK, Landstrom M. 2012. Non-Smad signaling pathways. Cell Tissue Res 347:11–20. http://dx.doi.org/10.1007/s00441-011-1201-y.
   PubMed Web of Science ®Google Scholar
• Verstrepen L, Verhelst K, Carpentier I, Beyaert R. 2011. TAX1BP1, a ubiquitin-binding adaptor protein in innate immunity and beyond. Trends Biochem Sci 36:347–354. http://dx.doi.org/10.1016/j.tibs.2011.03.004.
   PubMed Web of Science ®Google Scholar
• Wuerzberger-Davis SM, Miyamoto S. 2010. TAK-ling IKK activation: “Ub” the judge. Sci Signal 3:pe3. http://dx.doi.org/10.1126/scisignal.3105pe3.
   PubMedGoogle Scholar
• Xu P, Liu J, Derynck R. 2012. Post-translational regulation of TGF-β receptor and Smad signaling. FEBS Lett 586:1871–1884. http://dx.doi.org/10.1016/j.febslet.2012.05.010.
   PubMed Web of Science ®Google Scholar
• Ishitani T, Takaesu G, Ninomiya-Tsuji J, Shibuya H, Gaynor RB, Matsumoto K. 2003. Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling. EMBO J 22:6277–6288. http://dx.doi.org/10.1093/emboj/cdg605.
   PubMed Web of Science ®Google Scholar
• Landstrom M. 2010. The TAK1-TRAF6 signaling pathway. Int J Biochem Cell Biol 42:585–589. http://dx.doi.org/10.1016/j.biocel.2009.12.023.
   PubMed Web of Science ®Google Scholar
• Sakurai H. 2012. Targeting of TAK1 in inflammatory disorders and cancer. Trends Pharmacol Sci 33:522–530. http://dx.doi.org/10.1016/j.tips.2012.06.007.
   PubMed Web of Science ®Google Scholar
• Skaug B, Jiang X, Chen ZJ. 2009. The role of ubiquitin in NF-κB regulatory pathways. Annu Rev Biochem 78:769–796. http://dx.doi.org/10.1146/annurev.biochem.78.070907.102750.
   PubMed Web of Science ®Google Scholar
• Clague MJ, Liu H, Urbe S. 2012. Governance of endocytic trafficking and signaling by reversible ubiquitylation. Dev Cell 23:457–467. http://dx.doi.org/10.1016/j.devcel.2012.08.011.
   PubMed Web of Science ®Google Scholar
• Corn JE, Vucic D. 2014. Ubiquitin in inflammation: the right linkage makes all the difference. Nat Struct Mol Biol 21:297–300. http://dx.doi.org/10.1038/nsmb.2808.
   PubMed Web of Science ®Google Scholar
• MacGurn JA, Hsu PC, Emr SD. 2012. Ubiquitin and membrane protein turnover: from cradle to grave. Annu Rev Biochem 81:231–259. http://dx.doi.org/10.1146/annurev-biochem-060210-093619.
   PubMed Web of Science ®Google Scholar
• Polo S. 2012. Signaling-mediated control of ubiquitin ligases in endocytosis. BMC Biol 10:25. http://dx.doi.org/10.1186/1741-7007-10-25.
   PubMedGoogle Scholar
• Raiborg C, Stenmark H. 2009. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458:445–452. http://dx.doi.org/10.1038/nature07961.
   PubMed Web of Science ®Google Scholar
• Merrill JC, You J, Constable C, Leeman SE, Amar S. 2011. Whole-body deletion of LPS-induced TNF-α factor (LITAF) markedly improves experimental endotoxic shock and inflammatory arthritis. Proc Natl Acad Sci U S A 108:21247–21252. http://dx.doi.org/10.1073/pnas.1111492108.
   PubMedGoogle Scholar
• Moriwaki Y, Begum NA, Kobayashi M, Matsumoto M, Toyoshima K, Seya T. 2001. Mycobacterium bovis Bacillus Calmette-Guerin and its cell wall complex induce a novel lysosomal membrane protein, SIMPLE, that bridges the missing link between lipopolysaccharide and p53-inducible gene, LITAF(PIG7), and estrogen-inducible gene, EET-1. J Biol Chem 276:23065–23076. http://dx.doi.org/10.1074/jbc.M011660200.
   PubMedGoogle Scholar
• Srinivasan S, Leeman SE, Amar S. 2010. Beneficial dysregulation of the time course of inflammatory mediators in lipopolysaccharide-induced tumor necrosis factor alpha factor-deficient mice. Clin Vaccine Immunol 17:699–704. http://dx.doi.org/10.1128/CVI.00510-09.
   PubMedGoogle Scholar
• Chung JY, Park YC, Ye H, Wu H. 2002. All TRAFs are not created equal: common and distinct molecular mechanisms of TRAF-mediated signal transduction. J Cell Sci 115:679–688.
   PubMed Web of Science ®Google Scholar
• Xie P. 2013. TRAF molecules in cell signaling and in human diseases. J Mol Signal 8:7. http://dx.doi.org/10.1186/1750-2187-8-7.
   PubMedGoogle Scholar
• Jiang Z, Ninomiya-Tsuji J, Qian Y, Matsumoto K, Li X. 2002. Interleukin-1 (IL-1) receptor-associated kinase-dependent IL-1-induced signaling complexes phosphorylate TAK1 and TAB2 at the plasma membrane and activate TAK1 in the cytosol. Mol Cell Biol 22:7158–7167. http://dx.doi.org/10.1128/MCB.22.20.7158-7167.2002.
   PubMedGoogle Scholar
• Takaesu G, Kishida S, Hiyama A, Yamaguchi K, Shibuya H, Irie K, Ninomiya-Tsuji J, Matsumoto K. 2000. TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Mol Cell 5:649–658. http://dx.doi.org/10.1016/S1097-2765(00)80244-0.
   PubMed Web of Science ®Google Scholar
• Wang C, Deng L, Hong M, Akkaraju GR, Inoue J, Chen ZJ. 2001. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412:346–351. http://dx.doi.org/10.1038/35085597.
   PubMed Web of Science ®Google Scholar
• Ninomiya-Tsuji J, Kishimoto K, Hiyama A, Inoue J, Cao Z, Matsumoto K. 1999. The kinase TAK1 can activate the NIK-I κB as well as the MAP kinase cascade in the IL-1 signaling pathway. Nature 398:252–256. http://dx.doi.org/10.1038/18465.
   PubMed Web of Science ®Google Scholar
• Seet LF, Liu N, Hanson BJ, Hong W. 2004. Endofin recruits TOM1 to endosomes. J Biol Chem 279:4670–4679.
   PubMedGoogle Scholar
• Shibuya H, Yamaguchi K, Shirakabe K, Tonegawa A, Gotoh Y, Ueno N, Irie K, Nishida E, Matsumoto K. 1996. TAB1: an activator of the TAK1 MAPKKK in TGF-β signal transduction. Science 272:1179–1182. http://dx.doi.org/10.1126/science.272.5265.1179.
   PubMed Web of Science ®Google Scholar
• Sorrentino A, Thakur N, Grimsby S, Marcusson A, von Bulow V, Schuster N, Zhang S, Heldin CH, Landstrom M. 2008. The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner. Nat Cell Biol 10:1199–1207. http://dx.doi.org/10.1038/ncb1780.
   PubMed Web of Science ®Google Scholar
• Yamashita M, Fatyol K, Jin C, Wang X, Liu Z, Zhang YE. 2008. TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-beta. Mol Cell 31:918–924. http://dx.doi.org/10.1016/j.molcel.2008.09.002.
   PubMed Web of Science ®Google Scholar
• Kang JS, Liu C, Derynck R. 2009. New regulatory mechanisms of TGF-beta receptor function. Trends Cell Biol 19:385–394. http://dx.doi.org/10.1016/j.tcb.2009.05.008.
   PubMed Web of Science ®Google Scholar
• Massague J. 2012. TGFβ signaling in context. Nat Rev Mol Cell Biol 13:616–630. http://dx.doi.org/10.1038/nrm3434.
   PubMed Web of Science ®Google Scholar
• Moustakas A, Heldin CH. 2009. The regulation of TGFβ signal transduction. Development 136:3699–3714. http://dx.doi.org/10.1242/dev.030338.
   PubMed Web of Science ®Google Scholar
• Newton-Cheh C, Eijgelsheim M, Rice KM, de Bakker PI, Yin X, Estrada K, Bis JC, Marciante K, Rivadeneira F, Noseworthy PA, Sotoodehnia N, Smith NL, Rotter JI, Kors JA, Witteman JC, Hofman A, Heckbert SR, O'Donnell AG, Uitterlinden CJ, Psaty BM, Lumley T, Larson MG, Stricker BH. 2009. Common variants at ten loci influence QT interval duration in the QTGEN Study. Nat Genet 41:399–406. http://dx.doi.org/10.1038/ng.364.
   PubMed Web of Science ®Google Scholar
• Pfeufer A, Sanna S, Arking DE, Muller M, Gateva V, Fuchsberger C, Ehret GB, Orru M, Pattaro C, Kottgen A, Perz S, Usala G, Barbalic M, Li M, Putz B, Scuteri A, Prineas RJ, Sinner MF, Gieger C, Najjar SS, Kao WH, Muhleisen TW, Dei M, Happle C, Mohlenkamp S, Crisponi L, Erbel R, Jockel KH, Naitza S, Steinbeck G, Marroni F, Hicks AA, Lakatta E, Muller-Myhsok B, Pramstaller PP, Wichmann HE, Schlessinger D, Boerwinkle E, Meitinger T, Uda M, Coresh J, Kaab S, Abecasis GR, Chakravarti A. 2009. Common variants at ten loci modulate the QT interval duration in the QTSCD Study. Nat Genet 41:407–414. http://dx.doi.org/10.1038/ng.362.
   PubMed Web of Science ®Google Scholar
• Bertolo C, Roa S, Sagardoy A, Mena-Varas M, Robles EF, Martinez-Ferrandis JI, Sagaert X, Tousseyn T, Orta A, Lossos IS, Amar S, Natkunam Y, Briones J, Melnick A, Malumbres R, Martinez-Climent JA. 2013. LITAF, a BCL6 target gene, regulates autophagy in mature B-cell lymphomas. Br J Haematol 162:621–630. http://dx.doi.org/10.1111/bjh.12440.
   PubMed Web of Science ®Google Scholar
• Wang D, Liu J, Tang K, Xu Z, Xiong X, Rao Q, Wang M, Wang J. 2009. Expression of pig7 gene in acute leukemia and its potential to modulate the chemosensitivity of leukemic cells. Leuk Res 33:28–38. http://dx.doi.org/10.1016/j.leukres.2008.06.034.
   PubMedGoogle Scholar
• Zhou J, Yang Z, Tsuji T, Gong J, Xie J, Chen C, Li W, Amar S, Luo Z. 2011. LITAF and TNFSF15, two downstream targets of AMPK, exert inhibitory effects on tumor growth. Oncogene 30:1892–1900. http://dx.doi.org/10.1038/onc.2010.575.
   PubMedGoogle Scholar
• Behrends C, Harper JW. 2011. Constructing and decoding unconventional ubiquitin chains. Nat Struct Mol Biol 18:520–528. http://dx.doi.org/10.1038/nsmb.2066.
   PubMed Web of Science ®Google Scholar
• Kommaddi RP, Shenoy SK. 2013. Arrestins and protein ubiquitination. Prog Mol Biol Transl Sci 118:175–204. http://dx.doi.org/10.1016/B978-0-12-394440-5.00007-3.
   PubMed Web of Science ®Google Scholar
• Shukla AK, Xiao K, Lefkowitz RJ. 2011. Emerging paradigms of beta-arrestin-dependent seven transmembrane receptor signaling. Trends Biochem Sci 36:457–469. http://dx.doi.org/10.1016/j.tibs.2011.06.003.
   PubMed Web of Science ®Google Scholar
• Tian X, Kang DS, Benovic JL. 2014. beta-arrestins and G protein-coupled receptor trafficking. Handb Exp Pharmacol 219:173–186. http://dx.doi.org/10.1007/978-3-642-41199-1_9.
   PubMedGoogle Scholar
• Becuwe M, Herrador A, Haguenauer-Tsapis R, Vincent O, Leon S. 2012. Ubiquitin-mediated regulation of endocytosis by proteins of the arrestin family. Biochem Res Int 2012:242764. http://dx.doi.org/10.1155/2012/242764.
   PubMedGoogle Scholar
• Puca L, Brou C. 2014. Alpha-arrestins: new players in Notch and GPCR signaling pathways in mammals. J Cell Sci 127:1359–1367. http://dx.doi.org/10.1242/jcs.142539.
   PubMedGoogle Scholar
• Rauch S, Martin-Serrano J. 2011. Multiple interactions between the ESCRT machinery and arrestin-related proteins: implications for PPXY-dependent budding. J Virol 85:3546–3556. http://dx.doi.org/10.1128/JVI.02045-10.
   PubMedGoogle Scholar
• Puca L, Chastagner P, Meas-Yedid V, Israel A, Brou C. 2013. α-Arrestin 1 (ARRDC1) and β-arrestins cooperate to mediate Notch degradation in mammals. J Cell Sci 126:4457–4468. http://dx.doi.org/10.1242/jcs.130500.
   PubMedGoogle Scholar
• Huotari J, Helenius A. 2011. Endosome maturation. EMBO J 30:3481–3500. http://dx.doi.org/10.1038/emboj.2011.286.
   PubMed Web of Science ®Google Scholar
• Mittelbrunn M, Sanchez-Madrid F. 2012. Intercellular communication: diverse structures for exchange of genetic information. Nat Rev Mol Cell Biol 13:328–335. http://dx.doi.org/10.1038/nrm3335.
   PubMed Web of Science ®Google Scholar
• Simons M, Raposo G. 2009. Exosomes–vesicular carriers for intercellular communication. Curr Opin Cell Biol 21:575–581. http://dx.doi.org/10.1016/j.ceb.2009.03.007.
   PubMed Web of Science ®Google Scholar
• Katoh M. 2013. Therapeutics targeting angiogenesis: genetics and epigenetics, extracellular miRNAs and signaling networks. Int J Mol Med 32:763–767. http://dx.doi.org/10.3892/ijmm.2013.1444.
   PubMed Web of Science ®Google Scholar
• Sheldon H, Heikamp E, Turley H, Dragovic R, Thomas P, Oon CE, Leek R, Edelmann M, Kessler B, Sainson RC, Sargent I, Li JL, Harris AL. 2010. New mechanism for Notch signaling to endothelium at a distance by Delta-like 4 incorporation into exosomes. Blood 116:2385–2394. http://dx.doi.org/10.1182/blood-2009-08-239228.
   PubMed Web of Science ®Google Scholar
• Kuo L, Freed EO. 2012. ARRDC1 as a mediator of microvesicle budding. Proc Natl Acad Sci U S A 109:4025–4026. http://dx.doi.org/10.1073/pnas.1201441109.
   PubMed Web of Science ®Google Scholar
• Nabhan JF, Hu R, Oh RS, Cohen SN, Lu Q. 2012. Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein. Proc Natl Acad Sci U S A 109:4146–4151. http://dx.doi.org/10.1073/pnas.1200448109.
   PubMed Web of Science ®Google Scholar
• Bhoj VG, Chen ZJ. 2009. Ubiquitylation in innate and adaptive immunity. Nature 458:430–437. http://dx.doi.org/10.1038/nature07959.
   PubMed Web of Science ®Google Scholar
• Blanc C, Charette SJ, Mattei S, Aubry L, Smith EW, Cosson P, Letourneur F. 2009. Dictyostelium Tom1 participates to an ancestral ESCRT-0 complex. Traffic 10:161–171. http://dx.doi.org/10.1111/j.1600-0854.2008.00855.x.
   PubMedGoogle Scholar
• Herman EK, Walker G, van der Giezen M, Dacks JB. 2011. Multivesicular bodies in the enigmatic amoeboflagellate Breviata anathema and the evolution of ESCRT 0. J Cell Sci 124:613–621. http://dx.doi.org/10.1242/jcs.078436.
   PubMedGoogle Scholar
• Yamakami M, Yoshimori T, Yokosawa H. 2003. Tom1, a VHS domain-containing protein, interacts with Tollip, ubiquitin, and clathrin. J Biol Chem 278:52865–52872. http://dx.doi.org/10.1074/jbc.M306740200.
   PubMedGoogle Scholar
• Tang X, Metzger D, Leeman S, Amar S. 2006. LPS-induced TNF-alpha factor (LITAF)-deficient mice express reduced LPS-induced cytokine: evidence for LITAF-dependent LPS signaling pathways. Proc Natl Acad Sci U S A 103:13777–13782. http://dx.doi.org/10.1073/pnas.0605988103.
   PubMed Web of Science ®Google Scholar
• Luttrell LM. 2014. Minireview: more than just a hammer: ligand “bias” and pharmaceutical discovery. Mol Endocrinol 28:281–294. http://dx.doi.org/10.1210/me.2013-1314.
   PubMedGoogle Scholar
• Shukla AK. 2014. Biasing GPCR signaling from inside. Sci Signal 7:pe3. http://dx.doi.org/10.1126/scisignal.2005021.
   PubMedGoogle Scholar
• Wisler JW, Xiao K, Thomsen AR, Lefkowitz RJ. 2014. Recent developments in biased agonism. Curr Opin Cell Biol 27:18–24. http://dx.doi.org/10.1016/j.ceb.2013.10.008.
   PubMed Web of Science ®Google Scholar
• Carr R, III, Du Y, Quoyer J, Panettieri RA, Jr, Janz JM, Bouvier M, Kobilka BK, Benovic JL. 2014. Development and characterization of pepducins as Gs-biased allosteric agonists. J Biol Chem 289:35668–35684. http://dx.doi.org/10.1074/jbc.M114.618819.
   PubMed Web of Science ®Google Scholar
• Chakir K, Depry C, Dimaano VL, Zhu WZ, Vanderheyden M, Bartunek J, Abraham TP, Tomaselli GF, Liu SB, Xiang YK, Zhang M, Takimoto E, Dulin N, Xiao RP, Zhang J, Kass DA. 2011. Gαs-biased β2-adrenergic receptor signaling from restoring synchronous contraction in the failing heart. Sci Transl Med 3:100ra188. http://dx.doi.org/10.1126/scitranslmed.3001909.
   Google Scholar
• Nobles KN, Xiao K, Ahn S, Shukla AK, Lam CM, Rajagopal S, Strachan RT, Huang TY, Bressler EA, Hara MR, Shenoy SK, Gygi SP, Lefkowitz RJ. 2011. Distinct phosphorylation sites on the β2-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin. Sci Signal 4:ra51. http://dx.doi.org/10.1126/scisignal.2001707.
   PubMedGoogle Scholar
• Violin JD, Crombie AL, Soergel DG, Lark MW. 2014. Biased ligands at G-protein-coupled receptors: promise and progress. Trends Pharmacol Sci 35:308–316. http://dx.doi.org/10.1016/j.tips.2014.04.007.
   PubMed Web of Science ®Google Scholar
• Nohe A, Keating E, Knaus P, Petersen NO. 2004. Signal transduction of bone morphogenetic protein receptors. Cell Signal 16:291–299. http://dx.doi.org/10.1016/j.cellsig.2003.08.011.
   PubMed Web of Science ®Google Scholar
• Wotton D, Massague J. 2001. Smad transcriptional corepressors in TGF beta family signaling. Curr Top Microbiol Immunol 254:145–164.
   PubMedGoogle Scholar
• Kitisin K, Saha T, Blake T, Golestaneh N, Deng M, Kim C, Tang Y, Shetty K, Mishra B, Mishra L. 2007. TGF-β signaling in development. Sci STKE 2007:cm1.
   PubMedGoogle Scholar
• Chance PF, Pleasure D. 1993. Charcot-Marie-Tooth syndrome. Arch Neurol 50:1180–1184. http://dx.doi.org/10.1001/archneur.1993.00540110060006.
   PubMedGoogle Scholar
• Potulska-Chromik A, Sinkiewicz-Darol E, Kostera-Pruszczyk A, Drac H, Kabzinska D, Zakrzewska-Pniewska B, Golebiowski M, Kochanski A. 2012. Charcot-Marie-Tooth type 1C disease coexisting with progressive multiple sclerosis: a study of an overlapping syndrome. Folia Neuropathol 50:369–374.
   PubMedGoogle Scholar
• Bird TD. 1998. Charcot-Marie-Tooth neuropathy type 1. In Pagon RA, Bird TD, Dolan CR, Stephens K, Adam MP, Ardinger HH, Wallace SE, Amemiya A, Bean LJH, Fong C-T, Smith RJH (ed), GeneReviews. GeneReviews, Seattle, WA. http://www.ncbi.nlm.nih.gov/books/NBK1205/.
   Google Scholar
• Chance PF. 2004. Genetic evaluation of inherited motor/sensory neuropathy. Suppl Clin Neurophysiol 57:228–242. http://dx.doi.org/10.1016/S1567-424X(09)70360-5.
   PubMedGoogle Scholar