JBC Focus on PI3-Kinase with Echelon

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on May 24, 2002
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
277/22/19831    most recent
M109613200v1
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 Chuang, J.-Z.
Right arrow Articles by Sung, C.-H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chuang, J.-Z.
Right arrow Articles by Sung, C.-H.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print March 14, 2002
J. Biol. Chem, 10.1074/jbc.M109613200
Submitted on October 4, 2001
Revised on March 12, 2002
Accepted on March 14, 2002

Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently

Jen-Zen Chuang, Hui Zhou, Meicai Zhu, Shi-Hua Li, Xiao-Jiang Li, and Ching-Hwa Sung

Department of Ophthalmology, Weill Medical College of Cornell University, New York, NY 10021

Corresponding Author: chsung{at}mail.med.cornell.edu

Molecular chaperones are involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. DnaK- and DnaJ-like proteins are the two major classes of molecular chaperones in mammals. Recent studies have shown that DnaJ-like family proteins can inhibit polyglutamine aggregation, a hallmark of many neurodegenerative diseases including Huntington disease. While most DnaJ-like proteins studied are ubiquitously expressed, some have restricted expression, so it is possible that some specific chaperones may affect polyglutamine aggregation in specific neurons. In this report, we describe the isolation of a DnaJ-like protein MRJ and the characterization of its chaperone activity. Tissue distribution studies showed that MRJ is highly enriched in the central nervous system. In an in vitro cell model of Huntington disease (HD), overexpressed MRJ effectively suppressed polyglutamine-dependent protein aggregation, caspase activity, and cellular toxicity. Collectively, these results suggest that MRJ has a relevant functional role in neurons.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 DevelopmentHome page
E. D. Watson, C. Geary-Joo, M. Hughes, and J. C. Cross
The Mrj co-chaperone mediates keratin turnover and prevents the formation of toxic inclusion bodies in trophoblast cells of the placenta
Development, May 1, 2007; 134(9): 1809 - 1817.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
Y.-S. Dai, J. Xu, and J. D. Molkentin
The DnaJ-Related Factor Mrj Interacts with Nuclear Factor of Activated T Cells c3 and Mediates Transcriptional Repression through Class II Histone Deacetylase Recruitment
Mol. Cell. Biol., November 15, 2005; 25(22): 9936 - 9948.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Helmlinger, J. Bonnet, J.-L. Mandel, Y. Trottier, and D. Devys
Hsp70 and Hsp40 Chaperones Do Not Modulate Retinal Phenotype in SCA7 Mice
J. Biol. Chem., December 31, 2004; 279(53): 55969 - 55977.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
D. G. Hay, K. Sathasivam, S. Tobaben, B. Stahl, M. Marber, R. Mestril, A. Mahal, D. L. Smith, B. Woodman, and G. P. Bates
Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
Hum. Mol. Genet., July 1, 2004; 13(13): 1389 - 1405.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
Q. Chen, P. G. Vekilov, R. L. Nagel, and R. E. Hirsch
Liquid-Liquid Phase Separation in Hemoglobins: Distinct Aggregation Mechanisms of the {beta}6 Mutants
Biophys. J., March 1, 2004; 86(3): 1702 - 1712.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. C. Miller, L. A. Swayne, L. Chen, Z.-P. Feng, J. L. Wacker, P. J. Muchowski, G. W. Zamponi, and J. E. A. Braun
Cysteine String Protein (CSP) Inhibition of N-type Calcium Channels Is Blocked by Mutant Huntingtin
J. Biol. Chem., December 26, 2003; 278(52): 53072 - 53081.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
H. Adachi, M. Katsuno, M. Minamiyama, C. Sang, G. Pagoulatos, C. Angelidis, M. Kusakabe, A. Yoshiki, Y. Kobayashi, M. Doyu, et al.
Heat Shock Protein 70 Chaperone Overexpression Ameliorates Phenotypes of the Spinal and Bulbar Muscular Atrophy Transgenic Mouse Model by Reducing Nuclear-Localized Mutant Androgen Receptor Protein
J. Neurosci., March 15, 2003; 23(6): 2203 - 2211.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.