Regulating extracellular proteostasis capacity through the unfolded protein response

Prion

Volumn 9, Issue 1, 2015, Pages 10-21

  Genereux, Joseph C ^a   Wiseman, R Luke ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Amyloid disease; Extracellular chaperones; Protein aggregation; Proteostasis; Unfolded protein response

Indexed keywords

CHAPERONE; ERDJ3 CHAPERONE; GLUCOSE REGULATED PROTEIN 78; PREALBUMIN; PRION PROTEIN; UNCLASSIFIED DRUG; DNAJB11 PROTEIN, HUMAN; HEAT SHOCK PROTEIN 40; MEMBRANE PROTEIN;

AMYLOIDOSIS; ARTICLE; ENDOPLASMIC RETICULUM STRESS; EXTRACELLULAR SPACE; GENE OVEREXPRESSION; HUMAN; METABOLIC REGULATION; NONHUMAN; PATHOPHYSIOLOGY; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN HOMEOSTASIS; PROTEIN SECRETION; SIGNAL TRANSDUCTION; TRANSCRIPTION REGULATION; UNFOLDED PROTEIN RESPONSE; ANIMAL; BIOLOGICAL MODEL; CHEMISTRY; METABOLISM; PROTEIN CONFORMATION; SECRETION (PROCESS);

ANIMALS; ENDOPLASMIC RETICULUM STRESS; EXTRACELLULAR SPACE; HSP40 HEAT-SHOCK PROTEINS; HUMANS; MEMBRANE PROTEINS; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; PROTEIN CONFORMATION; UNFOLDED PROTEIN RESPONSE;

EID: 84954204422     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.1080/19336896.2015.1011887     Document Type: Article

References (52)

1. Blancas-Mejia LM, Ramirez-Alvarado M. Systemic amyloidoses. Annu Rev Biochem 2013; 82: 745-74; PMID: 23451869; http: //dx. doi. org/10. 1146/annurevbiochem-072611-130030
2. Kraus A, Groveman BR, Caughey B. Prions and the potential transmissibility of protein misfolding diseases. Annu Rev Microbiol 2013; 67: 543-64; PMID: 23808331; http: //dx. doi. org/10. 1146/annurevmicro-092412-155735
3. Knowles TP, Vendruscolo M, Dobson CM. The amyloid state and its association with protein misfolding diseases. Nat Rev Mol Cell Biol 2014; 15(6): 384-96; PMID: 24854788; http: //dx. doi. org/10. 1038/nrm3810
4. Wyatt AR, Yerbury JJ, Ecroyd H, Wilson MR. Extracellular chaperones and proteostasis. Annu Rev Biochem 2013; 82: 295-322; PMID: 23350744; http: //dx. doi. org/10. 1146/annurev-biochem-072711-163904
5. Schwarzman AL, Gregori L, Vitek MP, Lyubski S, Strittmatter WJ, Enghilde JJ, Bhasin R, Silverman J, Weisgraber KH, Coyle PK et al. Transthyretin sequesters amyloid beta protein and prevents amyloid formation. Proc Natl Acad Sci U S A 1994; 91 (18): 8368-72; PMID: 8078889; http: //dx. doi. org/ 10. 1073/pnas. 91. 18. 8368
6. Finn TE, Nunez AC, Sunde M, Easterbrook-Smith SB. Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligands. J Biol Chem 2012; 287(25): 21530-40; PMID: 22549788; http: //dx. doi. org/10. 1074/jbc. M112. 372961
7. Traut TW. Physiological concentrations of purines and pyrimidines. Mol Cell Biochem 1994; 140(1): 1-22; PMID: 7877593; http: //dx. doi. org/10. 1007/ BF00928361
8. Schwiebert EM, Zsembery A. Extracellular ATP as a signaling molecule for epithelial cells. Biochim Biophys Acta 2003; 1615(1-2): 7-32; PMID: 12948585; http: //dx. doi. org/10. 1016/S0005-2736(03)00210-4
9. Nuutinen T, Huuskonen J, Suuronen T, Ojala J, Miettinen R, Salminen A. Amyloid-beta 1-42 induced endocytosis and clusterin/apoJ protein accumulation in cultured human astrocytes. Neurochem Int 2007; 50(3): 540-7; PMID: 17196306; http: //dx. doi. org/ 10. 1016/j. neuint. 2006. 11. 002
10. Wyatt AR, Yerbury JJ, Berghofer P, Greguric I, Katsifis A, Dobson CM, Wilson MR. Clusterin facilitates in vivo clearance of extracellular misfolded proteins. Cell Mol Life Sci 2011; 68(23): 3919-31; PMID: 21505792; http: //dx. doi. org/10. 1007/s00018-011-0684-8
11. Soltys BJ, Gupta RS. Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells. Exp Cell Res 1996; 222(1): 16-27; PMID: 8549659; http: //dx. doi. org/ 10. 1006/excr. 1996. 0003
12. Martins I, Kepp O, Galluzzi L, Senovilla L, Schlemmer F, Adjemian S, Menger L, Michaud M, Zitvogel L, Kroemer G. Surface-exposed calreticulin in the interaction between dying cells and phagocytes. Ann N Y Acad Sci 2010; 1209: 77-82; PMID: 20958319; http: //dx. doi. org/10. 1111/j. 1749-6632. 2010. 05740. x
13. Zhang Y, Liu R, Ni M, Gill P, Lee AS. Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/ BiP. J Biol Chem 2010; 285(20): 15065-15075; PMID: 20208072; http: //dx. doi. org/10. 1074/jbc. M109. 087445
14. Peters LR, Raghavan M. Endoplasmic reticulum calcium depletion impacts chaperone secretion, innate immunity, and phagocytic uptake of cells. J Immunol 2011; 187(2): 919-31; http: //dx. doi. org/10. 4049/ jimmunol. 1100690
15. Lee AS. Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential. Nat Rev Cancer 2014; 14(4): 263-76; PMID: 24658275; http: // dx. doi. org/10. 1038/nrc3701
16. Holtzman DM. In vivo effects of ApoE and clusterin on amyloid-beta metabolism and neuropathology. J Mol Neurosci 2004; 23(3): 247-54; PMID: 15181253; http: //dx. doi. org/10. 1385/JMN: 23: 3: 247
17. Magalhaes J, Saraiva MJ. Clusterin overexpression and its possible protective role in transthyretin deposition in familial amyloidotic polyneuropathy. J Neuropathol Exp Neurol 2011; 70(12): 1097-1106; PMID: 22082661; http: //dx. doi. org/10. 1097/ NEN. 0b013e31823a44f4
18. Greene MJ, Sam F, Soo Hoo PT, Patel RS, Seldin DC, Connors LH. Evidence for a functional role of the molecular chaperone clusterin in amyloidotic cardiomyopathy. Am J Pathol 2011; 178(1): 61-8; PMID: 21224044; http: //dx. doi. org/10. 1016/j. ajpath. 2010. 11. 015
19. Magalhaes J, Saraiva MJ. The heat shock response in FAP: the role of the extracellular chaperone clusterin. Amyloid 2012; 19 Suppl 1: 3-4; PMID: 22512538; http: //dx. doi. org/10. 3109/13506129. 2012. 675370
20. McGeer PL, Kawamata T, Walker DG. Distribution of clusterin in Alzheimer brain tissue. Brain Res 1992; 579(2): 337-41; PMID: 1378350; http: //dx. doi. org/10. 1016/0006-8993(92)90071-G
21. Freixes M, B Puig A Rodriguez B Torrejon-Escribano R, Blanco I. Ferrer. Clusterin solubility and aggregation in Creutzfeldt-Jakob disease. Acta Neuropathol 2004; 108(4): 295-301; PMID: 15235804; http: //dx. doi. org/10. 1007/s00401-004-0891-6
22. Braakman I, Bulleid NJ. Protein folding and modification in the mammalian endoplasmic reticulum. Annu Rev Biochem 2011; 80: 71-99; PMID: 21495850; http: //dx. doi. org/10. 1146/annurev-biochem-062209-093836
23. Guerriero CJ, Brodsky JL. The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology. Physiol Rev 2012; 92(2): 537-76; PMID: 22535891; http: //dx. doi. org/10. 1152/physrev. 00027. 2011
24. Ryno LM, Wiseman RL, Kelly JW. Targeting unfolded protein response signaling pathways to ameliorate protein misfolding diseases. Curr Opin Chem Biol 2013; 17(3): 346-52; PMID: 23647985; http: //dx. doi. org/10. 1016/j. cbpa. 2013. 04. 009
25. Buxbaum JN. The systemic amyloidoses. Curr Opin Rheumatol 2004; 16(1): 67-75; PMID: 14673392; http: //dx. doi. org/10. 1097/00002281-200401000-00013
26. Wiseman RL, Koulov A, Powers E, Kelly JW, Balch WE. Protein energetics in maturation of the early secretory pathway. Curr Opin Cell Biol 2007; 19 (4): 359-367; PMID: 17686625; http: //dx. doi. org/ 10. 1016/j. ceb. 2007. 05. 005
27. Sekijima Y, Wiseman RL, Matteson J, Hammarstrom P, Miller SR, Sawkar AR, Balch WE, Kelly JW. The biological and chemical basis for tissue-selective amyloid disease. Cell 2005; 121(1): 73-85; PMID: 15820680; http: //dx. doi. org/10. 1016/j. cell. 2005. 01. 018
28. Gidalevitz T, Ho KH, Brignull HR, Morimoto RI. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 2006; 311 (5766): 1471-4; PMID: 16469881; http: //dx. doi. org/ 10. 1126/science. 1124514
29. Hutt DM, Powers ET, Balch WE. The proteostasis boundary in misfolding diseases of membrane traffic. FEBS Lett 2009; 583(16): 2639-46; PMID: 19708088; http: //dx. doi. org/10. 1016/j. febslet. 2009. 07. 014
30. 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
31. Gidalevitz T, Kikis EA, Morimoto RI. A cellular perspective on conformational disease: the role of genetic background and proteostasis networks. Curr Opin Struct Biol 2010; 20(1): 23-32; PMID: 20053547; http: //dx. doi. org/10. 1016/j. sbi. 2009. 11. 001
32. Brehme M, Voisine C, Rolland T, Wachi S, Soper JH, Zhu Y, Orton K, Villella A, Garza D, Vidal M, Ge H, Morimoto RI. A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. Cell Rep 2014; 9(3): 1135-50; PMID: 25437566; http: //dx. doi. org/10. 1016/j. celrep. 2014. 09. 042
33. Hipp MS, Park SH, Hartl FU. Proteostasis impairment in protein-misfolding and-aggregation diseases. Trends Cell Biol 2014; 24(9): 506-14; PMID: 24946960; http: //dx. doi. org/10. 1016/j. tcb. 2014. 05. 003
34. Han J, Back SH, Hur J, Lin YH, Gildersleeve R, Shan J, Yuan CL, Krokowski D, Wang S, Hatzoglou M, Kilberg MS, Sartor MA, Kaufman RJ. ER-stressinduced transcriptional regulation increases protein synthesis leading to cell death. Nat Cell Biol 2013; 15(5): 481-90; PMID: 23624402; http: //dx. doi. org/ 10. 1038/ncb2738
35. Satpute-Krishnan P, Ajinkya M, Bhat S, Itakura E, Hegde RS, Lippincott-Schwartz J. ER stress-induced clearance of misfolded GPI-anchored proteins via the secretory pathway. Cell 2014; 158(3): 522-33; PMID: 25083867; http: //dx. doi. org/10. 1016/j. cell. 2014. 06. 026
36. Hetz C, Mollereau B. Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat Rev Neurosci 2014; 15(4): 233-49; PMID: 24619348; http: //dx. doi. org/10. 1038/nrn3689
37. Walter P, Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011; 334(6059): 1081-6; PMID: 22116877; http: //dx. doi. org/10. 1126/science. 1209038
38. Shoulders MD, Ryno LM, Genereux JC, Moresco JJ, Tu PG, Wu C, Yates 3rd JR, Su AI, Kelly JW, Wiseman RL. Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments. Cell Rep 2013; 3 (4): 1279-92; PMID: 23583182; http: //dx. doi. org/ 10. 1016/j. celrep. 2013. 03. 024
39. Chen JJ, Genereux JC, Qu S, Hulleman JD, Shoulders MD, Wiseman RL. ATF6 activation reduces the secretion and extracellular aggregation of destabilized variants of an amyloidogenic protein. Chem Biol 2014; 21: 1564-74; PMID: 25444553; http: //dx. doi. org/10. 1016/j. chembiol. 2014. 09. 009
40. Cooley CB, Ryno LM, Plate L, Morgan GJ, Hulleman JD, Kelly JW, Wiseman RL. Unfolded protein response activation reduces secretion and extracellular aggregation of amyloidogenic immunoglobulin light chain. Proc Natl Acad Sci U S A 2014; 111 (36): 13046-51; PMID: 25157167; http: //dx. doi. org/ 10. 1073/pnas. 1406050111
41. Nizard P, Tetley S, Le Drean Y, Watrin T, Le Goff P, Wilson MR, Michel D. Stress-induced retrotranslocation of clusterin/ApoJ into the cytosol. Traffic 2007; 8(5): 554-65; PMID: 17451556; http: //dx. doi. org/ 10. 1111/j. 1600-0854. 2007. 00549. x
42. Genereux JC, Qu S, Zhou M, Ryno LM, Wang S, Shoulders MD, Kaufman RJ, Lasmezas CI, Kelly JW, Wiseman RL. Unfolded protein responseinduced ERdj3 secretion links ER stress to extracellular proteostasis. EMBO J 2015; 34(1): 4-19; PMID: 25361606; http: //dx. doi. org/10. 15252/embj. 201488896
43. Shen Y, Hendershot LM. ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates. Mol Biol Cell 2005; 16(1): 40-50; PMID: 15525676; http: //dx. doi. org/10. 1091/mbc. E04-05-0434
44. Jin Y, AwadW, Petrova K, Hendershot LM. Regulated release of ERdj3 from unfolded proteins by BiP. EMBO J 2008; 27(21): 2873-82; PMID: 18923428; http: //dx. doi. org/10. 1038/emboj. 2008. 207
45. Tan YL, Genereux JC, Pankow S, Aerts JM, Yates JR 3rd, Kelly JW. ERdj3 is an endoplasmic reticulum degradation factor for mutant glucocerebrosidase variants linked to Gaucher's disease. Chem Biol 2014; 21(8): 967-76; PMID: 25126989; http: //dx. doi. org/ 10. 1016/j. chembiol. 2014. 06. 008
46. Otero JH, Lizak B, Feige MJ, Hendershot LM. Dissection of structural and functional requirements that underlie the interaction of ERdj3 protein with substrates in the endoplasmic reticulum. J Biol Chem 2014; 289(40): 27504-12; PMID: 25143379; http: //dx. doi. org/10. 1074/jbc. M114. 587147
47. Yerbury JJ, Poon S, Meehan S, Thompson B, Kumita JR, Dobson CM, Wilson MR. The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J 2007; 21(10): 2312-22; PMID: 17412999; http: //dx. doi. org/10. 1096/fj. 06-7986com
48. Yerbury JJ, Kumita JR, Meehan S, Dobson CM, Wilson MR. Alpha2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species. J Biol Chem 2009; 284 (7): 4246-54; PMID: 19074141; http: //dx. doi. org/ 10. 1074/jbc. M807242200
49. Narayan P, Orte A, Clarke RW, Bolognesi B, Hook S, Ganzinger KA, Meehan S, Wilson MR, Dobson CM, Klenerman D. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-beta (1-40) peptide. Nat Struct Mol Biol 2012; 19(1): 79-83; http: //dx. doi. org/10. 1038/nsmb. 2191
50. Zhou M, Ottenberg G, Sferrazza GF, Lasmezas CI. Highly neurotoxic monomeric alpha-helical prion protein. Proc Natl Acad Sci U S A 2012; 109 (8): 3113-3118; PMID: 22323583; http: //dx. doi. org/ 10. 1073/pnas. 1118090109
51. Taylor RC, Dillin A. Aging as an event of proteostasis collapse. Cold Spring Harb Perspect Biol 2011; 3 (5): PMID: 21441594; http: //dx. doi. org/10. 1101/ cshperspect. a004440
52. Calamini B, Morimoto RI. Protein homeostasis as a therapeutic target for diseases of protein conformation. Curr Top Med Chem 2012; 12(22): 2623-40; PMID: 23339312; http: //dx. doi. org/10. 2174/1568026 611212220014