FASEB J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
20/6/741
05-5080fjev1    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Marques, C.
Right arrow Articles by Shang, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Marques, C.
Right arrow Articles by Shang, F.
The FASEB Journal Express Article doi:10.1096/fj.05-5080fje
Published online February 9, 2006

The triage of damaged proteins: degradation by the ubiquitin-proteasome pathway or repair by molecular chaperones

Carla Marques, Weimin Guo, Paulo Pereira, Allen Taylor, Cam Patterson, Paul C. Evans, and Fu Shang

E-mail contact: fu.shang{at}tufts.edu

Accumulation of damaged proteins is causally related to many age-related diseases. The ubiquitin-proteasome pathway (UPP) plays a role in selective degradation of damaged proteins, whereas molecular chaperones, such as heat shock proteins, are involved in refolding denatured proteins. This work demonstrates for the first time that the UPP and molecular chaperones work in a competitive manner and that the fates of denatured proteins are determined by the relative activities of the UPP and molecular chaperones. Enhanced UPP activity suppresses the refolding of denatured proteins whereas elevated chaperone activity inhibits the degradation of denatured proteins. CHIP, a co-chaperone with E3 activity, plays a pivotal role in determining the fates of the damaged proteins. The delicate balance between UPP-mediated degradation and refolding of denatured proteins is governed by relative levels of CHIP and other molecular chaperones. Isopeptidases, the enzymes that reverse the actions of CHIP, also play an important role in determining the fate of denatured proteins.

Key words: CHIP • heat shock proteins • isopeptidase • luciferase




This article has been cited by other articles:


Home page
 IOVSHome page
X. Zhang, J. Zhou, A. F. Fernandes, J. R. Sparrow, P. Pereira, A. Taylor, and F. Shang
The Proteasome: A Target of Oxidative Damage in Cultured Human Retina Pigment Epithelial Cells
Invest. Ophthalmol. Vis. Sci., August 1, 2008; 49(8): 3622 - 3630.
[Abstract] [Full Text] [PDF]

Home page
 IOVSHome page
X. Zhang, E. J. Dudek, B. Liu, L. Ding, A. F. Fernandes, J. J. Liang, J. Horwitz, A. Taylor, and F. Shang
Degradation of C-terminal Truncated {alpha}A-crystallins by the Ubiquitin Proteasome Pathway
Invest. Ophthalmol. Vis. Sci., September 1, 2007; 48(9): 4200 - 4208.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
H. Adachi, M. Waza, K. Tokui, M. Katsuno, M. Minamiyama, F. Tanaka, M. Doyu, and G. Sobue
CHIP Overexpression Reduces Mutant Androgen Receptor Protein and Ameliorates Phenotypes of the Spinal and Bulbar Muscular Atrophy Transgenic Mouse Model
J. Neurosci., May 9, 2007; 27(19): 5115 - 5126.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
M. S. M. Oakley, S. Kumar, V. Anantharaman, H. Zheng, B. Mahajan, J. D. Haynes, J. K. Moch, R. Fairhurst, T. F. McCutchan, and L. Aravind
Molecular Factors and Biochemical Pathways Induced by Febrile Temperature in Intraerythrocytic Plasmodium falciparum Parasites
Infect. Immun., April 1, 2007; 75(4): 2012 - 2025.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2006 by The Federation of American Societies for Experimental Biology.