14-3-3 and aggresome formation : Implications in neurodegenerative diseases

Prion

Volumn 8, Issue 2, 2014, Pages 173-177

  Jia, Baohui ^a,b   Wu, Yuying ^a   Zhou, Yi ^a  

^a FLORIDA STATE UNIVERSITY COLLEGE OF MEDICINE   (United States)

^b INSTITUTE OF CHINESE MATERIA MEDICA   (China)

Author keywords

14 3 3; Aggresomes; Chaperones; Inclusion bodies; Neurodegeneration; Protein aggregation; Protein misfolding

Indexed keywords

BCL 2 ASSOCIATED ATHANOGENE 3; CHAPERONE; DYNEIN ADENOSINE TRIPHOSPHATASE; HEAT SHOCK PROTEIN 70; PROTEIN; PROTEIN 14 3 3; UNCLASSIFIED DRUG;

AGGRESOME; DEGENERATIVE DISEASE; HUMAN; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN TARGETING; PROTEIN TRANSPORT; REVIEW; PATHOPHYSIOLOGY; PHYSIOLOGY;

14-3-3 PROTEINS; HUMANS; NEURODEGENERATIVE DISEASES; PROTEIN FOLDING;

EID: 84907525554     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.28123     Document Type: Review

References (52)

1. Balch WE, Morimoto RI, Dillin A, Kelly JW. Adapting proteostasis for disease intervention. Science 2008; 319:916-9; PMID:18276881; http:// dx.doi.org/10.1126/science.1141448
2. Gregersen N. Protein misfolding disorders: pathogenesis and intervention. J Inherit Metab Dis 2006; 29:456-70; PMID:16763918; http://dx.doi.org/10.1007/s10545-006-0301-4
3. Powers ET, Morimoto RI, Dillin A, Kelly JW, Balch WE. Biological and chemical approaches to diseases of proteostasis deficiency. Annu Rev Biochem 2009; 78:959-91; PMID:19298183; http://dx.doi.org/10.1146/annurev.biochem.052308.114844
4. Kopito RR. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000; 10:524- 30; PMID:11121744; http://dx.doi.org/10.1016/ S0962-8924(00)01852-3
5. Gamerdinger M, Carra S, Behl C. Emerging roles of molecular chaperones and co-chaperones in selective autophagy: focus on BAG proteins. J Mol Med (Berl) 2011; 89:1175-82; PMID:21818581; http://dx.doi.org/10.1007/s00109-011-0795-6
6. Garcia-Mata R, Gao YS, Sztul E. Hassles with taking out the garbage: aggravating aggresomes. Traffic 2002; 3:388-96; PMID:12010457; http://dx.doi.org/10.1034/j.1600-0854.2002.30602.x
7. Tyedmers J, Mogk A, Bukau B. Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 2010; 11:777-88; PMID:20944667; http:// dx.doi.org/10.1038/nrm2993
8. Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell 2006; 125:443-51; PMID:16678092; http://dx.doi.org/10.1016/j.cell.2006.04.014
9. Stetler RA, Gan Y, Zhang W, Liou AK, Gao Y, Cao G, Chen J. Heat shock proteins: cellular and molecular mechanisms in the central nervous system. Prog Neurobiol 2010; 92:184-211; PMID:20685377; http://dx.doi.org/10.1016/j.pneurobio.2010.05.002
10. Nandi D, Tahiliani P, Kumar A, Chandu D. The ubiquitin-proteasome system. J Biosci 2006; 31:137- 55; PMID:16595883; http://dx.doi.org/10.1007/ BF02705243
11. Chin LS, Olzmann JA, Li L. Parkin-mediated ubiquitin signalling in aggresome formation and autophagy. Biochem Soc Trans 2010; 38:144- 9; PMID:20074049; http://dx.doi.org/10.1042/ BST0380144
12. García-Mata R, Bebök Z, Sorscher EJ, Sztul ES. Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J Cell Biol 1999; 146:1239-54; PMID:10491388; http://dx.doi.org/10.1083/jcb.146.6.1239
13. Johnston JA, Ward CL, Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol 1998; 143:1883-98; PMID:9864362; http://dx.doi.org/10.1083/jcb.143.7.1883
14. Lamark T, Johansen T. Aggrephagy: selective disposal of protein aggregates by macroautophagy. Int J Cell Biol 2012; 2012:736905; PMID:22518139; http:// dx.doi.org/10.1155/2012/736905
15. Nixon RA. The role of autophagy in neurodegenerative disease. Nat Med 2013; 19:983-97; PMID:23921753; http://dx.doi.org/10.1038/nm.3232
16. Taylor JP, Tanaka F, Robitschek J, Sandoval CM, Taye A, Markovic-Plese S, Fischbeck KH. Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein. Hum Mol Genet 2003; 12:749-57; PMID:12651870; http://dx.doi.org/10.1093/hmg/ddg074
17. Moore BEP. V.J. Specific acidic proteins of the nervous system. In: F.D. Carlson EC, ed. Physiological and Biochemical Aspects of Nervous Integration. NJ: Prentice Hall, 1967:343-59
18. Rosenquist M, Sehnke P, Ferl RJ, Sommarin M, Larsson C. Evolution of the 14-3-3 protein family: does the large number of isoforms in multicellular organisms reflect functional specificity? J Mol Evol 2000; 51:446-58; PMID:11080367
19. Muslin AJ, Tanner JW, Allen PM, Shaw AS. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 1996; 84:889-97; PMID:8601312; http://dx.doi.org/10.1016/S0092-8674(00)81067-3
20. Fu H, Subramanian RR, Masters SC. 14-3-3 proteins: structure, function, and regulation. Annu Rev Pharmacol Toxicol 2000; 40:617-47; PMID:10836149; http://dx.doi.org/10.1146/ annurev.pharmtox.40.1.617
21. Berg D, Holzmann C, Riess O. 14-3-3 proteins in the nervous system. Nat Rev Neurosci 2003; 4:752-62; PMID:12951567; http://dx.doi.org/10.1038/nrn1197
22. Waelter S, Boeddrich A, Lurz R, Scherzinger E, Lueder G, Lehrach H, Wanker EE. Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol Biol Cell 2001; 12:1393-407; PMID:11359930; http://dx.doi.org/10.1091/mbc.12.5.1393
23. Wang Y, Meriin AB, Zaarur N, Romanova NV, Chernoff YO, Costello CE, Sherman MY. Abnormal proteins can form aggresome in yeast: aggresometargeting signals and components of the machinery. FASEB J 2009; 23:451-63; PMID:18854435; http:// dx.doi.org/10.1096/fj.08-117614
24. Omi K, Hachiya NS, Tanaka M, Tokunaga K, Kaneko K. 14-3-3zeta is indispensable for aggregate formation of polyglutamine-expanded huntingtin protein. Neurosci Lett 2008; 431:45-50; PMID:18078716; http://dx.doi.org/10.1016/j.neulet.2007.11.018
25. Xu Z, Graham K, Foote M, Liang F, Rizkallah R, Hurt M, Wang Y, Wu Y, Zhou Y. 14-3-3 protein targets misfolded chaperone-associated proteins to aggresomes. J Cell Sci 2013; 126:4173-86; PMID:23843611; http://dx.doi.org/10.1242/ jcs.126102
26. Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, Yao TP. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 2003; 115:727- 38; PMID:14675537; http://dx.doi.org/10.1016/ S0092-8674(03)00939-5
27. Olzmann JA, Chin LS. Parkin-mediated K63-linked polyubiquitination: a signal for targeting misfolded proteins to the aggresome-autophagy pathway. Autophagy 2008; 4:85-7; PMID:17957134
28. Braselmann S, McCormick F. Bcr and Raf form a complex in vivo via 14-3-3 proteins. EMBO J 1995; 14:4839-48; PMID:7588613
29. Vincenz C, Dixit VM. 14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules. J Biol Chem 1996; 271:20029-34; PMID:8702721; http://dx.doi.org/10.1074/jbc.271.33.20029
30. Gamerdinger M, Kaya AM, Wolfrum U, Clement AM, Behl C. BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins. EMBO Rep 2011; 12:149- 56; PMID:21252941; http://dx.doi.org/10.1038/ embor.2010.203
31. Dokladny K, Zuhl MN, Mandell M, Bhattacharya D, Schneider S, Deretic V, Moseley PL. Regulatory coordination between two major intracellular homeostatic systems: heat shock response and autophagy. J Biol Chem 2013; 288:14959-72; PMID:23576438; http://dx.doi.org/10.1074/jbc. M113.462408
32. Zhang X, Qian SB. Chaperone-mediated hierarchical control in targeting misfolded proteins to aggresomes. Mol Biol Cell 2011; 22:3277-88; PMID:21775628;
33. Broadley SA, Hartl FU. The role of molecular chaperones in human misfolding diseases. FEBS Lett 2009; 583:2647-53; PMID:19393652; http://dx.doi.org/10.1016/j.febslet.2009.04.029
34. Arias E, Cuervo AM. Chaperone-mediated autophagy in protein quality control. Curr Opin Cell Biol 2011; 23:184-9; PMID:21094035; http:// dx.doi.org/10.1016/j.ceb.2010.10.009
35. Gamerdinger M, Hajieva P, Kaya AM, Wolfrum U, Hartl FU, Behl C. Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG EMBO J 2009; 28:889-901; PMID:19229298; http://dx.doi.org/10.1038/ emboj.2009.29
36. Meriin AB, Gabai VL, Yaglom J, Shifrin VI, Sherman MY. Proteasome inhibitors activate stress kinases and induce Hsp Diverse effects on apoptosis. J Biol Chem 1998; 273:6373-9; PMID:9497367; http:// dx.doi.org/10.1074/jbc.273.11.6373
37. Kyriakis JM, Avruch J. Protein kinase cascades activated by stress and inflammatory cytokines. Bioessays 1996; 18:567-77; PMID:8757935; http:// dx.doi.org/10.1002/bies.950180708
38. Watabe M, Nakaki T. Protein kinase CK2 regulates the formation and clearance of aggresomes in response to stress. J Cell Sci 2011; 124:1519-32; PMID:21486957; http://dx.doi.org/10.1242/ jcs.081778
39. Watabe M, Nakaki T. CK2 as anti-stress factor. Commun Integr Biol 2012; 5:278-80; PMID:22896792; http://dx.doi.org/10.4161/ cib.19473
40. Tran PB, Miller RJ. Aggregates in neurodegenerative disease: crowds and power? Trends Neurosci 1999; 22:194-7; PMID:10322490; http://dx.doi.org/10.1016/S0166-2236(99)01409-5
41. Kawamoto Y, Akiguchi I, Nakamura S, Honjyo Y, Shibasaki H, Budka H. 14-3-3 proteins in Lewy bodies in Parkinson disease and diffuse Lewy body disease brains. J Neuropathol Exp Neurol 2002; 61:245-53; PMID:11895039
42. Ubl A, Berg D, Holzmann C, Krüger R, Berger K, Arzberger T, Bornemann A, Riess O. 14-3-3 protein is a component of Lewy bodies in Parkinson's disease-mutation analysis and association studies of 14-3-3 eta. Brain Res Mol Brain Res 2002; 108:33- 9; PMID:12480176; http://dx.doi.org/10.1016/ S0169-328X(02)00510-7
43. Layfield R, Fergusson J, Aitken A, Lowe J, Landon M, Mayer RJ. Neurofibrillary tangles of Alzheimer's disease brains contain 14-3-3 proteins. Neurosci Lett 1996; 209:57-60; PMID:8734909; http://dx.doi.org/10.1016/0304-3940(96)12598-2
44. Umahara T, Uchihara T, Tsuchiya K, Nakamura A, Iwamoto T, Ikeda K, Takasaki M. 14-3-3 proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease. Acta Neuropathol 2004; 108:279-86; PMID:15235803; http://dx.doi.org/10.1007/s00401-004-0885-4
45. Okamoto Y, Shirakashi Y, Ihara M, Urushitani M, Oono M, Kawamoto Y, Yamashita H, Shimohama S, Kato S, Hirano A, et al. Colocalization of 14-3-3 proteins with SOD1 in Lewy body-like hyaline inclusions in familial amyotrophic lateral sclerosis cases and the animal model. PLoS One 2011; 6:e20427; PMID:21655264; http://dx.doi.org/10.1371/journal.pone.0020427
46. Foote M, Zhou Y. 14-3-3 proteins in neurological disorders. Int J Biochem Mol Biol 2012; 3:152-64; PMID:22773956
47. Steinacker P, Aitken A, Otto M. 14-3-3 proteins in neurodegeneration. Semin Cell Dev Biol 2011; 22:696-704; PMID:21920445; http://dx.doi.org/10.1016/j.semcdb.2011.08.005
48. Kaneko K, Hachiya NS. The alternative role of 14-3-3 zeta as a sweeper of misfolded proteins in disease conditions. Med Hypotheses 2006; 67:169- 71; PMID:16516399; http://dx.doi.org/10.1016/j. mehy.2006.01.019
49. Bodner RA, Outeiro TF, Altmann S, Maxwell MM, Cho SH, Hyman BT, McLean PJ, Young AB, Housman DE, Kazantsev AG. Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases. Proc Natl Acad Sci U S A 2006; 103:4246-51; PMID:16537516; http://dx.doi.org/10.1073/ pnas.0511256103
50. Milroy LG, Brunsveld L, Ottmann C. Stabilization and inhibition of protein-protein interactions: the 14-3-3 case study. ACS Chem Biol 2013; 8:27- 35; PMID:23210482; http://dx.doi.org/10.1021/ cb300599t
51. Zhao J, Meyerkord CL, Du Y, Khuri FR, Fu H. 14-3-3 proteins as potential therapeutic targets. Semin Cell Dev Biol 2011; 22:705-12; PMID:21983031; http:// dx.doi.org/10.1016/j.semcdb.2011.09.012
52. Olzmann JA, Li L, Chin LS. Aggresome formation and neurodegenerative diseases: therapeutic implications. Curr Med Chem 2008; 15:47-60; PMID:18220762;