The proteostasis boundary in misfolding diseases of membrane traffic

FEBS Letters

Volumn 583, Issue 16, 2009, Pages 2639-2646

  Hutt, Darren M ^a   Powers, Evan T ^a   Balch, William E ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Membrane trafficking; Protein folding; Proteostasis

Indexed keywords

CHAPERONE; DIPEPTIDYL PEPTIDASE IV INHIBITOR; EXENDIN 4; HEAT SHOCK PROTEIN; HISTONE DEACETYLASE INHIBITOR; PROTEASOME; PROTEOME; UBIQUITIN; UNCLASSIFIED DRUG; VX 770;

ALZHEIMER DISEASE; AMYLOIDOSIS; CELL ENERGY; CELL TYPE; CYSTIC FIBROSIS; DEGENERATIVE DISEASE; DEMYELINATING DISEASE; DRUG MECHANISM; DRUG SCREENING; ENDOCYTOSIS; ENVIRONMENTAL FACTOR; EPIGENETICS; EUKARYOTIC CELL; EXOCYTOSIS; GENE MUTATION; HOMEOSTASIS; HUMAN; KINETICS; LIGHT CHAIN; LOSS OF FUNCTION MUTATION; LYSOSOME STORAGE DISEASE; MEMBRANE BIOLOGY; MEMBRANE TRANSPORT; MYELOMA; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN TRANSPORT; REGULATORY MECHANISM; SHORT SURVEY; SIGNAL TRANSDUCTION; THERMODYNAMICS; TISSUE REACTION; TRANSCRIPTION REGULATION;

CELL MEMBRANE; HUMANS; METABOLIC DISEASES; METABOLIC NETWORKS AND PATHWAYS; NEURODEGENERATIVE DISEASES; PROTEIN FOLDING; PROTEIN TRANSPORT; PROTEINS;

EUKARYOTA;

EID: 68649100255     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.07.014     Document Type: Short Survey

References (78)

1. Balch W.E., Morimoto R.I., Dillin A., and Kelly J.W. Adapting proteostasis for disease intervention. Science 319 (2008) 916-919
2. Malhotra J.D., and Kaufman R.J. The endoplasmic reticulum and the unfolded protein response. Semin. Cell Dev. Biol. 18 (2007) 716-731
3. Ron D., and Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8 (2007) 519-529
4. Lin J.H., Walter P., and Yen T.S. Endoplasmic reticulum stress in disease pathogenesis. Annu. Rev. Pathol. 3 (2008) 399-425
5. Morimoto R.I. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 22 (2008) 1427-1438
6. Shamovsky I., and Nudler E. New insights into the mechanism of heat shock response activation. Cell Mol. Life Sci. 65 (2008) 855-861
7. Petersen O.H., Michalak M., and Verkhratsky A. Calcium signalling: past, present and future. Cell Calcium 38 (2005) 161-169
8. Burdakov D., Petersen O.H., and Verkhratsky A. Intraluminal calcium as a primary regulator of endoplasmic reticulum function. Cell Calcium 38 (2005) 303-310
9. Medzhitov R. Origin and physiological roles of inflammation. Nature 454 (2008) 428-435
10. Zhang K., and Kaufman R.J. From endoplasmic-reticulum stress to the inflammatory response. Nature 454 (2008) 455-462
11. Gregor M.G., and Hotamisligil G.S. Adipocyte stress: the endoplasmic reticulum and metabolic disease. J. Lipid Res. 48 (2007) 1905-1914
12. Hotamisligil G.S. Inflammation and metabolic disorders. Nature 444 (2006) 860-867
13. Wellen K.E., and Hotamisligil G.S. Inflammation, stress, and diabetes. J. Clin. Invest. 115 (2005) 1111-1119
14. Braun P., Rietman E., and Vidal M. Networking metabolites and diseases. Proc. Natl. Acad. Sci. USA 105 (2008) 9849-9850
15. Goh K.I., Cusick M.E., Valle D., Childs B., Vidal M., and Barabasi A.L. The human disease network. Proc. Natl. Acad. Sci. USA 104 (2007) 8685-8690
16. Ideker T., and Sharan R. Protein networks in disease. Genome Res. 18 (2008) 644-652
17. Powers E.T., Morimoto R.I., Dillin A., Kelly J.W., and Balch W.E. Biological and chemical approaches to diseases of proteostasis deficiency. Annu. Rev. Biochem. 78 (2009) 959-991
18. Young J.C., Agashe V.R., Siegers K., and Hartl F.U. Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev. Mol. Cell Biol. 5 (2004) 781-791
19. Konstantinova I.M., Tsimokha A.S., and Mittenberg A.G. Role of proteasomes in cellular regulation. Int. Rev. Cell Mol. Biol. 267 (2008) 59-124
20. Tasaki T., and Kwon Y.T. The mammalian N-end rule pathway: new insights into its components and physiological roles. Trends Biochem. Sci. 32 (2007) 520-528
21. Levine B., and Kroemer G. Autophagy in the pathogenesis of disease. Cell 132 (2008) 27-42
22. Kundu M., and Thompson C.B. Autophagy: basic principles and relevance to disease. Annu. Rev. Pathol. 3 (2008) 427-455
23. Prahlad V., Cornelius T., and Morimoto R.I. Regulation of the cellular heat shock response in Caenorhabditis elegans by thermosensory neurons. Science 320 (2008) 811-814
24. Murphy K.G., and Bloom S.R. Gut hormones and the regulation of energy homeostasis. Nature 444 (2006) 854-859
25. Dill K.A., Ozkan S.B., Shell M.S., and Weikl T.R. The protein folding problem. Annu. Rev. Biophys. 37 (2008) 289-316
26. Das R., and Baker D. Macromolecular modeling with rosetta. Annu. Rev. Biochem. 77 (2008) 363-382
27. Sekijima Y., Wiseman R.L., Matteson J., Hammarstrom P., Miller S.R., Sawkar A.R., Balch W.E., and Kelly J.W. The biological and chemical basis for tissue-selective amyloid disease. Cell 121 (2005) 73-85
28. Wiseman R.L., Powers E.T., Buxbaum J.N., Kelly J.W., and Balch W.E. An adaptable standard for protein export from the endoplasmic reticulum. Cell 131 (2007) 809-821
29. Brignull H.R., Morley J.F., and Morimoto R.I. The stress of misfolded proteins: C. elegans models for neurodegenerative disease and aging. Adv. Exp. Med. Biol. 594 (2007) 167-189
30. Gidalevitz T., Ben-Zvi A., Ho K.H., Brignull H.R., and Morimoto R.I. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311 (2006) 1471-1474
31. Appenzeller-Herzog C., and Ellgaard L. The human PDI family: versatility packed into a single fold. Biochim. Biophys. Acta 1783 (2008) 535-548
32. Hanson S.R., Culyba E.K., Hsu T.L., Wong C.H., Kelly J.W., and Powers E.T. The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability. Proc. Natl. Acad. Sci. USA 106 (2009) 3131-3136
33. Gurkan C., Lapp H., Alory C., Su A.I., Hogenesch J.B., and Balch W.E. Large-scale profiling of Rab GTPase trafficking networks: the membrane. Mol. Biol. Cell 16 (2005) 3847-3864
34. Malhotra J.D., and Kaufman R.J. Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword?. Antioxid. Redox Signal. 9 (2007) 2277-2293
35. Pearl L.H., Prodromou C., and Workman P. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem. J. 410 (2008) 439-453
36. Workman P., Burrows F., Neckers L., and Rosen N. Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann. NY Acad. Sci. 1113 (2007) 202-216
37. Riordan J.R. CFTR function and prospects for therapy. Annu. Rev. Biochem. 77 (2008) 701-726
38. Qu B.H., Strickland E., and Thomas P.J. Cystic fibrosis: a disease of altered protein folding. J. Bioenerg. Biomembr. 29 (1997) 483-490
39. Wang X., et al. Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127 (2006) 803-815
40. Turnbull E.L., Rosser M.F., and Cyr D.M. The role of the UPS in cystic fibrosis. BMC Biochem. 8 Suppl. 1 (2007) S11
41. Boucher R.C. Evidence for airway surface dehydration as the initiating event in CF airway disease. J. Int. Med. 261 (2007) 5-16
42. Loo T.W., Bartlett M.C., and Clarke D.M. Correctors promote folding of the CFTR in the endoplasmic reticulum. Biochem. J. 413 (2008) 29-36
43. Conn P.M., Ulloa-Aguirre A., Ito J., and Janovick J.A. G protein-coupled receptor trafficking in health and disease: lessons learned to prepare for therapeutic mutant rescue in vivo. Pharmacol. Rev. 59 (2007) 225-250
44. Yu Z., Sawkar A.R., and Kelly J.W. Pharmacologic chaperoning as a strategy to treat Gaucher disease. FEBS J. 274 (2007) 4944-4950
45. Mu T.W., Ong D.S., Wang Y.J., Balch W.E., Yates III J.R., Segatori L., and Kelly J.W. Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell 134 (2008) 769-781
46. Hurshman Babbes A.R., Powers E.T., and Kelly J.W. Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between stability and amyloidosis. Biochemistry 47 (2008) 6969-6984
47. Tojo K., Sekijima Y., Kelly J.W., and Ikeda S. Diflunisal stabilizes familial amyloid polyneuropathy-associated transthyretin variant tetramers in serum against dissociation required for amyloidogenesis. Neurosci. Res. 56 (2006) 4419
48. Ulloa-Aguirre A., and Conn P.M. Targeting of G protein-coupled receptors to the plasma membrane in health and disease. Front Biosci. 14 (2009) 973-994
49. Aridor M. Visiting the ER: the endoplasmic reticulum as a target for therapeutics in traffic related diseases. Adv. Drug Deliv Rev. 59 (2007) 759-781
50. Lin W., and Popko B. Endoplasmic reticulum stress in disorders of myelinating cells. Nat. Neurosci. 12 (2009) 379-385
51. Bateman J.F., Boot-Handford R.P., and Lamande S.R. Genetic diseases of connective tissues: cellular and extracellular effects of ECM mutations. Nat. Rev. Genet. 10 (2009) 173-183
52. Kosmaoglou M., Schwarz N., Bett J.S., and Cheetham M.E. Molecular chaperones and photoreceptor function. Prog. Retin. Eye Res. 27 (2008) 434-449
53. Gent J., and Braakman I. Low-density lipoprotein receptor structure and folding. Cell Mol. Life Sci. 61 (2004) 2461-2470
54. Hinault M.P., Ben-Zvi A., and Goloubinoff P. Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging. J. Mol. Neurosci. 30 (2006) 249-265
55. Matus S., Lisbona F., Torres M., Leon C., Thielen P., and Hetz C. The stress rheostat: an interplay between the unfolded protein response (UPR) and autophagy in neurodegeneration. Curr. Mol. Med. 8 (2008) 157-172
56. Perlmutter D.H. Autophagic disposal of the aggregation-prone protein that causes liver inflammation and carcinogenesis in alpha-1-antitrypsin deficiency. Cell Death Differ. 16 (2009) 39-45
57. Malhotra J.D., Miao H., Zhang K., Wolfson A., Pennathur S., Pipe S.W., and Kaufman R.J. Antioxidants reduce endoplasmic reticulum stress and improve protein secretion. Proc. Natl. Acad. Sci. USA 105 (2008) 18525-18530
58. Kim P.S., et al. Defective protein folding and intracellular retention of thyroglobulin-R19K mutant as a cause of human congenital goiter. Mol. Endocrinol. 22 (2008) 477-484
59. Myllyharju J. Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets. Ann. Med. 40 (2008) 402-417
60. Comenzo R.L. Current and emerging views and treatments of systemic immunoglobulin light-chain (Al) amyloidosis. Contrib. Nephrol. 153 (2007) 195-210
61. Page L.J., Suk J.Y., Huff M.E., Lim H.J., Venable J., Yates J., Kelly J.W., and Balch W.E. Metalloendoprotease cleavage triggers gelsolin amyloidogenesis. EMBO J. 24 (2005) 4124-4132
62. Butters T.D. Gaucher disease. Curr. Opin. Chem. Biol. 11 (2007) 412-418
63. Comenzo R.L. Primary systemic amyloidosis. Curr. Treat. Options Oncol. 1 (2000) 83-89
64. Kahn S.E., Hull R.L., and Utzschneider K.M. Mechanisms linking obesity to insulin resistance and type 2 diabetes. Nature 444 (2006) 840-846
65. Panowski S.H., Wolff S., Aguilaniu H., Durieux J., and Dillin A. PHA-4/Foxa mediates diet-restriction-induced longevity of C. elegans. Nature 447 (2007) 550-555
66. Scheuner D., and Kaufman R.J. The unfolded protein response: a pathway that links insulin demand with beta-cell failure and diabetes. Endocr. Rev. 29 (2008) 317-333
67. Eizirik D.L., Cardozo A.K., and Cnop M. The role for endoplasmic reticulum stress in diabetes mellitus. Endocr. Rev. 29 (2008) 42-61
68. Haataja L., Gurlo T., Huang C.J., and Butler P.C. Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. Endocr. Rev. 29 (2008) 303-316
69. Hull R.L., Westermark G.T., Westermark P., and Kahn S.E. Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes. J. Clin. Endocrinol. Metab. 89 (2004) 3629-3643
70. Dashwood R.H., and Ho E. Dietary histone deacetylase inhibitors: from cells to mice to man. Semin. Cancer Biol. 17 (2007) 363-369
71. Ozcan U., Yilmaz E., Ozcan L., Furuhashi M., Vaillancourt E., Smith R.O., Gorgun C.Z., and Hotamisligil G.S. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 313 (2006) 1137-1140
72. Metoyer C.F., and Pruitt K. The role of sirtuin proteins in obesity. Pathophysiology 15 (2008) 103-108
73. Elliott P.J., and Jirousek M. Sirtuins: novel targets for metabolic disease. Curr. Opin. Investig. Drugs 9 (2008) 371-378
74. Bordone L., and Guarente L. Sirtuins and beta-cell function. Diabetes Obes. Metab. 9 Suppl. 2 (2007) 23-27
75. Milne J.C., et al. Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature 450 (2007) 712-716
76. Salehi M., Aulinger B.A., and D'Alessio D.A. Targeting beta-cell mass in type 2 diabetes: promise and limitations of new drugs based on incretins. Endocr. Rev. 29 (2008) 367-379
77. Halimi S. DPP-4 inhibitors and GLP-1 analogues: for whom? Which place for incretins in the management of type 2 diabetic patients?. Diabetes Metab. 34 Suppl. 2 (2008) S91-S95
78. Geller R., Vignuzzi M., Andino R., and Frydman J. Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev. 21 (2007) 195-205