Integration of endoplasmic reticulum signaling in health and disease

Nature Medicine

Volumn 5, Issue 7, 1999, Pages 745-

  Aridor, Meir ^a   Balch, William E ^a  

^a Salk institute for Biological Sciences   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE;

ALZHEIMER DISEASE; CYSTIC FIBROSIS; ENDOPLASMIC RETICULUM; HEMOCHROMATOSIS; HUMAN; LIGAND BINDING; NEUROPATHY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; REVIEW; SIGNAL TRANSDUCTION;

DISEASE; ENDOPLASMIC RETICULUM; HUMANS; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; SIGNAL TRANSDUCTION;

EID: 0345465663     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/10466     Document Type: Review

References (80)

1. Matlack, K.E., Mothes, W. & Rapoport, T.A. Protein translocation: tunnel vision. Cell 92, 381-390 (1998).
2. Trombetta, E.S. & Helenius, A. Lectins as chaperones in glycoprotein folding. Curr. Opin. Struct. Biol. 8, 587-592 (1998).
3. Liu, Y., Choudhury, P., Cabral, C.M. & Sifers, R.N. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. J. Biol. Chem. 274, 5861-5867 (1999).
4. Hammond, C. & Helenius, A. Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7, 523-529 (1995).
5. Chapman, R., Sidrauski, C. & Walter, P. Intracellular signaling from the endoplasmic reticulum to the nucleus. Annu. Rev. Cell. Dev. Biol. 14, 459-485 (1998).
6. Pahl, H.L. & Baeuerle, P.A. Endoplasmic reticulum induced signal transduction and gene expression. Trends Cell Biol. 7, 50-55 (1997).
7. Harding, H.P., Zhang, Y. & Ron, D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397, 271-274 (1999).
8. Pahl, H.L. & Baeuerle, P.A. The ER-overload response: activation of NF-kB. Trends Cell Biol. 22 63-67 (1997).
9. Wang, X.Z. & Ron, D. Stress-induced phosphorylation and activation of the transcription factor CHOP (Gadd153) by p38 MAP kinase. Science 272, 1347-1349 (1996).
10. Batchvarova, N., Wang, X.Z. & Ron, D. Inhibition of adipogenesis by the stress-induced protein CHOP (Gadd153). EMBO J. 14, 4654-4661 (1995).
11. Zinszner, H. et al. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev. 12, 982-995 (1998).
12. Aridor, M. & Balch, W.E. Principles of selective transport: coat complexes hold the key. Trends Cell Biol. 6, 315-320 (1996).
13. Aridor, M., Bannykh, S.I., Rowe, T. & Balch, W.E. Cargo can modulate COPII vesicle formation from the endoplasmic reticulum. J. Biol. Chem. 274, 4389-4399 (1999).
14. Schekman, R. & Orci, L. Coat proteins and vesicle budding. Science 271, 1526-1533 (1996).
15. Springer, S. & Schekman, S. Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs. Science 281, 698-700 (1998).
16. Aridor, M., Weissman, J., Bannykh, S., Nouffer, C. & Balch, W.E. Cargo selection by the COPII budding machinery during export from the endoplasmic reticulum. J. Cell Biol. 141, 61-70 (1998).
17. Bannykh, S.I., Rowe, T. & Balch, W.E. Organization of endoplasmic reticulum export complexes. J. Cell Biol. 135, 19-35 (1996).
18. Kaiser, C.A. & Schekman, R. Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell 61, 723-733 (1990).
19. Saito, Y., Yamanushi, T., Oka, T. & Nakano, A. Identification of SEC12, SED4, truncated SEC16, and EKS1/HRD3 as multicopy suppressors of ts mutants of Sar1 GTPase. J. Biochem. (Tokyo) 125, 130-137 (1999).
20. Zhen, L., Baumann, H., Novak, E.K. & Swank, R.T. The signal for retention of the egasyn-glucuronidase complex within the endoplasmic reticulum. Arch. Biochem. 304, 402-414 (1993).
21. Shelness, G.S., Ingram, M.F., Huang, X.F. & DeLozier, J.A. Apolipoprotein B in the rough endoplasmic reticulum: translation, translocation and the initiation of lipoprotein assembly. J. Nutr. 129, 456S-462S (1999).
22. Baker, E.K., Colley, N.J. & Zuker, C.S. The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J. 13, 4886-4895 (1994).
23. Bu, G. & Schwartz, A.L. RAP, a novel type of ER chaperone. Trends Cell Biol. 8, 272-276 (1998).
24. Kuehn, M.J., Hermann, M. & Schekman, R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature 391, 187-190 (1998).
25. Nishimura, N. & Balch, W.E. A di-acidic signal required for selective export from the endoplasmic reticulum. Science 277, 556-558 (1997).
26. Nishimura, N. et al. A di-acidic (DXE) code directs concentration of cargo during export from the endoplasmic reticulum. J. Biol. Chem. 274, 15937-15946 (1999).
27. Fiedler, K. & Rothman, J.E. Sorting determinants in the transmembrane domain of p24 proteins. J. Biol. Chem. 272, 24739-24742 (1997).
28. Kappeler, F., Klopfenstein, D.R., Foguet, M., Paccaud, J.P. & Hauri, H.P.The recycling of ERGIC-53 in the early secretory pathway. ERGIC-53 carries a cytosolic endoplasmic reticulum-exit determinant interacting with COPII. J. Biol. Chem. 272, 31801-31808 (1997).
29. Bannykh, S., Nishimura, N. & Balch, W.E.Getting into the Golgi. Trends Cell Biol. 8, 21-25 (1998).
30. Nichols, W.C. et al. Mutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII. Cell 93, 61-70 (1998).
31. White, A.L., Guerra, B. & Lanford, R.E. Influence of allelic variation on apolipoprotein (a) folding in the endoplasmic reticulum. J. Biol. Chem. 272, 5048-5055 (1997).
32. Kim, P.S. & Arvan, P. Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: disorders of protein trafficking and the role of ER molecular chaperones. Endocr Rev. 19, 173-202 (1998).
33. Macintyre, S., Samols, D. & Dailey, P. Two carboxylesterases bind C-reactive protein within the endoplasmic reticulum and regulate its secretion during the acute phase response. J. Biol. Chem. 269, 24496-24503 (1994).
34. Kuwana, T., Peterson, P.A. & Karlsson, L. Exit of major histocompatibility complex class II-invariant chain p35 complexes from the endoplasmic reticulum is modulated by phosphorylation. Proc. Natl. Acad. Sci. USA 95, 1056-1061 (1998).
35. Sommer, T. & Wolf, D.H. Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J. 11, 1227-1233 (1997).
36. Brodsky, J.L. & McCracken, A.A. ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol. 7, 151-156 (1997).
37. Johnston, J.A., Ward, C.L. & Kopito, R.R. Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143, 1883-1898 (1998).
38. Kopito, R.R. Biosynthesis and degradation of CFTR. Physiol. Rev. 79, S167-173 (1999).
39. Hardy, J. & Gwinn-Hardy, K. Genetic classification of primary neurodegenerative disease. Science 282, 1075-1079 (1998).
40. Gardner, R. et al. Sequence determinants for regulated degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell. 9, 2611-2626 (1998).
41. Nohturfft, A., Brown, M.S. & Goldstein, J.L. Sterols regulate processing of carbohydrate chains of wild-type SREBP cleavage-activating protein (SCAP), but not sterol-resistant mutants Y29BC or D443N. Proc Natl. Acad. Sci. USA 95, 12848-12853 (1998).
42. Ploegh, H.L. Viral strategies of immune evasion. Science 280, 248-253 (1998).
43. Margottin, F. et al. A novel human WD protein, h-betaTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Cell 1, 565-574 (1998).
44. Yaron, A. et al. Identification of the receptor component of the IkappaBalpha-ubiquitin ligase. Nature 396, 590-4 (1998).
45. Doedens, J.R., Giddings, J., T.H. & Kirkegaard, K. Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: genetic and ultrastructural analysis. J. Virol. 71, 9054-9064 (1997).
46. Lord, J.M. & Roberts, L.M. Toxin entry: retrograde transport through the secretory pathway. J. Cell Biol. 140, 733-736 (1998).
47. Simpson, J.C., Dascher, C., Roberts, L.M., Lord, J.M. & Balch, W.E. Ricin cytotoxicity is sensitive to recycling between the endoplasmic reticulum and the Golgi complex J. Biol. Chem. 270, 20078-20083 (1995).
48. Sandvig, K. et al. Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum. Nature 358, 510-512 (1992).
49. Kuhn, L. Iron overload: molecular clues to its cause. Trends Biochem. Sci. 24, 164-166 (1999).
50. Qu, D., Teckman, J.H. & Perlmutter, D.H. Alpha 1-antitrypsin deficiency associated liver disease. J. Gastroenterol. Hepatol. 12, 404-416 (1997).
51. Sifers, R.N., Finegold, M.J. & Woo, S.L.C. Molecular biology and genetics of alpha1-antitrypsin deficiency. Semin. Liver Dis. 12, 301-310 (1992).
52. Brooks, D.A. Protein processing: a role in the pathophysiology of genetic disease. FEBS Lett. 409, 115-120 (1997).
53. Kukuruzinska, M.A. & Lennon, K. Protein N-glycosylation: molecular genetics and functional significance. Crit Rev. Oral Biol. Med. 9, 415-448 (1998).
54. Kalin, N., Claabeta, A., Sommer, M., Puchelle, E. & Tummler, B. DeltaF508 CFTR protein expression in tissues from patients with cystic fibrosis. J. Clin. Invest 103, 1379-1389 (1999).
55. Prockop, D.J. & Kivirikko, K.I. Collagens: molecular biology, diseases, and potentials for therapy. Anna Rev. Biochem. 64, 403-434 (1995).
56. Hodes, M., Pratt, V. & Dlouhy, S. Genetics of Perlizaeus-Merzbacher disease. Devel. Neurosci. 15, 383-394 (1993).
57. Gow, A. & Lazzarini, R.A. A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease. Nature Genet. 13, 422-428 (1996).
58. Griffiths, I. et al. Axonal swellings and degeneration in mice lacking the major proteolipid of myelin. Science 280, 1610-1613 (1998).
59. Hodes, M.E. & Dlouby, S.R. The proteolipid protein gene: double, double, ....and trouble. Am. J. Genet. 59, 12-15 (1996).
60. De Jonghe, P., Timmerman, V., Nelis, E., Martin, J. & Van Broeckhoven, C. Charcot-Marie-Tooth disease and related peripheral neuropathies. J. Periph. Nervous Sys. 2, 370-387 (1997).
61. D'Urso, D., Prior, R., Greiner-Petter, R., Gabreels-Festen, A.A.W.M. & Muller, H.W. Overloaded endoplasmic reticulum-golgi compartments, a possible pathomechanism of peripheral neuropathies caused by mutations of the peripheral myelin protein PMP22. J. Neurosci. 18, 731-740 (1998).
62. Pruisner, S.B., Scott, M.R., DeArmond, S.J. & Cohen, F.E. Prion protein biology. Cell 93, 337-348 (1998).
63. Kelly, J.W. The alternative conformations of amyloidogenic proteins and their multistep assembly pathways. Curr. Opin. Struct. Biol. 8, 101-106 (1998).
64. Selkoe, D.J. The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell Biol. 8, 447-453 (1998).
65. Cook, D.G. et al. Alzheimer's ABeta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nature Med. 3, 1021-1023 (1997).
66. Mattson, M.P., Guo, Q., Furukawa, K. & Pedersen, W.A. Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease. J. Neurochem. 70, 1-14 (1998).
67. De Strooper, B. et al. deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391, 387-390 (1998).
68. De Strooper, B. et al. Phosphorylation, subcellular localization, and membrane orientation of the Alzheimer's disease-associated presenilins. J. Biol. Chem. 272, 3590-3598 (1997).
69. Culvenor, J.D. et al. Res. Alzheimer's disease associated presenilin 1 in neuronal cells: evidence for localization to the endoplasmic reticulum-Golgi intermediate compartment. J. Neurosci. 49, 719-731 (1997).
70. Haass, C. & Mandelkow, E. Proteolysis by presenilins and the renaissance of tau. Trends Cell Biol. 9, 241-244 (1999).
71. Wong, P.C. et al. Presenilin 1 is required for Notch1 and DII1 expression in the paraxial mesoderm. Nature 387, 288-292 (1997).
72. Artavanis-Tsakonas, S., Rand, M.D. & Lake, R.J. Notch signaling: cell fate control and signal integration in development. Science 284, 770-776 (1999).
73. Struhl, G. & Greenwald, I. Presenilin is required for activity and nuclear access of Notch in Drosophila. Nature 398, 522-525 (1999).
74. Chan, Y.M. & Jan, Y.N. Roles for proteolysis and trafficking in notch maturation and signal transduction. Cell 94, 423-426 (1998).
75. De Strooper, B. et al. A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain. Nature 398, 518-522 (1999).
76. Hampton, R.Y., Gardner, R.G. & Rine, J. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7, 2029-2044 (1996).
77. Mandelkow, E.M. & Mandelkow, E. Tau in Alzheimer's disease. Trends Cell Biol. 8, 425-427 (1998).
78. Loo, T.W. & Clarke, D.M. Correction of defective protein kinesis of human p-glycoprotein mutants by substrates and modulators. J. Biol. Chem. 272, 709-712 (1997).
79. c A2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. 271, 22796-22801 (1996).
80. Departments of Cell and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037