Prevention of aberrant protein aggregation by anchoring the molecular chaperone αb-crystallin to the endoplasmic reticulum

Biochemical and Biophysical Research Communications

Volumn 455, Issue 3-4, 2014, Pages 241-245

  Yamamoto, Shinichiro ^a   Yamashita, Arisa ^a   Arakaki, Naokatu ^a   Nemoto, Hisao ^a   Yamazaki, Tetsuo ^a  

^a UNIVERSITY OF TOKUSHIMA   (Japan)

Author keywords

Endoplasmic reticulum; Protein aggregation; R120G mutant; Crystallinopathy; B crystallin

Indexed keywords

BETA CRYSTALLIN; SMALL INTERFERING RNA; ALPHA CRYSTALLIN; CYCLOHEXIMIDE; GREEN FLUORESCENT PROTEIN; PROTEIN BINDING;

ALPHA CRYSTALLINOPATHY; ARTICLE; AUTOPHAGY; ENDOPLASMIC RETICULUM; EXPRESSION VECTOR; GENETIC TRANSFECTION; HELA CELL LINE; HUMAN; HUMAN CELL; HUMAN CELL CULTURE; IMMUNOCYTOCHEMISTRY; MICROENVIRONMENT; MUSCLE DISEASE; PREVENTION; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN EXPRESSION; CHEMISTRY; FLUORESCENCE MICROSCOPY; GENETICS; IMMUNOPRECIPITATION; METABOLISM; MUTATION; PATHOLOGY; PROTEIN AGGREGATION, PATHOLOGICAL;

ALPHA-CRYSTALLIN B CHAIN; AUTOPHAGY; CYCLOHEXIMIDE; ENDOPLASMIC RETICULUM; GREEN FLUORESCENT PROTEINS; HELA CELLS; HUMANS; IMMUNOPRECIPITATION; MICROSCOPY, FLUORESCENCE; MUSCULAR DISEASES; MUTATION; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN BINDING; RNA, SMALL INTERFERING; TRANSFECTION;

EID: 84914107633     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.10.151     Document Type: Article

References (27)

1. Y. Sun, and T.H. MacRae Small heat shock proteins: molecular structure and chaperone function Cell. Mol. Life Sci. 62 2005 2460 2476
2. D. Selcen, and A.G. Engel Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations Ann. Neurol. 54 2003 804 810
3. P. Reilich, B. Schoser, N. Schramm, S. Krause, J. Schessl, and W. Kress The p. G154S mutation of the alpha-B crystallin gene (CRYAB) causes late-onset distal myopathy Neuromuscul. Disord. 20 2010 255 259
4. P. Vicart, A. Caron, P. Guicheney, Z. Li, M.C. Prévost, and A. Faure A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy Nat. Genet. 20 1998 92 95
5. A.T. Chavez Zobel Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G αB-crystallin mutant Hum. Mol. Genet. 12 2003 1609 1620
6. M.D. Perng, P.J. Muchowski, P. van Den IJssel, G.J. Wu, A.M. Hutcheson, and J.I. Clark The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro J. Biol. Chem. 274 1999 33235 33243
7. A. Sanbe Molecular mechanisms of α-crystallinopathy and its therapeutic strategy Biol. Pharm. Bull. 34 2011 1653 1658
8. R.R. Kopito Aggresomes, inclusion bodies and protein aggregation Trends Cell Biol. 10 2000 524 530
9. F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
10. C. Xu, B. Bailly-Maitre, and J.C. Reed Endoplasmic reticulum stress: cell life and death decisions J. Clin. Invest. 115 2005 2656 2664
11. S. Escusa-Toret, W.I.M. Vonk, and J. Frydman Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress Nat. Cell Biol. 15 2013 1231 1243
12. S. Specht, S.B.M. Miller, A. Mogk, and B. Bukau Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae J. Cell Biol. 195 2011 617 629
13. X.-D. Liu, S. Ko, Y. Xu, E.A. Fattah, Q. Xiang, and C. Jagannath Transient aggregation of ubiquitinated proteins is a cytosolic unfolded protein response to inflammation and endoplasmic reticulum stress J. Biol. Chem. 287 2012 19687 19698
14. A. Yamashita, T. Taniwaki, Y. Kaikoi, and T. Yamazaki Protective role of the endoplasmic reticulum protein mitsugumin23 against ultraviolet C-induced cell death FEBS Lett. 587 2013 1299 1303
15. S. Yamamoto, T. Yamazaki, S. Komazaki, T. Yamashita, M. Osaki, and M. Matsubayashi Contribution of calumin to embryogenesis through participation in the endoplasmic reticulum-associated degradation activity Dev. Biol. 393 2014 33 43
16. J. Tyedmers, A. Mogk, and B. Bukau Cellular strategies for controlling protein aggregation Nat. Rev. Mol. Cell Biol. 11 2010 777 788
17. M.S. Hipp, S.-H. Park, and F.U. Hartl Proteostasis impairment in protein-misfolding and -aggregation diseases Trends Cell Biol. 24 2014 506 514
18. E.M. Sontag, W.I.M. Vonk, and J. Frydman Sorting out the trash: the spatial nature of eukaryotic protein quality control Curr. Opin. Cell Biol. 26 2014 139 146
19. N.P. Dantuma, and L.C. Bott The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution Front. Mol. Neurosci. 7 2014 1 18
20. A. Hershko, and A. Ciechanover The ubiquitin system Annu. Rev. Biochem. 67 1998 425 479
21. Y. Ohsumi Molecular dissection of autophagy: two ubiquitin-like systems Nat. Rev. Mol. Cell Biol. 2 2001 211 216
22. A. Kuma, M. Hatano, M. Matsui, A. Yamamoto, H. Nakaya, and T. Yoshimori The role of autophagy during the early neonatal starvation period Nature 432 2004 1032 1036
23. T. Hara, K. Nakamura, M. Matsui, A. Yamamoto, Y. Nakahara, and R. Suzuki-Migishima Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice Nature 441 2006 885 889
24. J. Kirstein-Miles, A. Scior, E. Deuerling, and R.I. Morimoto The nascent polypeptide-associated complex is a key regulator of proteostasis EMBO J. 32 2013 1451 1468
25. L.G. Goldfarb, M. Olivé, P. Vicart, and H.H. Goebel Intermediate filament diseases: desminopathy Adv. Exp. Med. Biol. 642 2008 131 164
26. R.I. Morimoto, and A.M. Cuervo Proteostasis and the aging proteome in health and disease J. Gerontol. A Biol. Sci. Med. Sci. 69 Suppl. 1 2014 S33 S38
27. Y.E. Kim, M.S. Hipp, A. Bracher, M. Hayer-Hartl, and F.U. Hartl Molecular chaperone functions in protein folding and proteostasis Annu. Rev. Biochem. 82 2013 323 355