| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 277, Issue 22, 19831-19838, May 31, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the 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's disease (HD). Although 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 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.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF426743.
Characterization of a Brain-enriched Chaperone, MRJ, That
Inhibits Huntingtin Aggregation and Toxicity Independently*
§,
,**
Department of Ophthalmology and
** Department of Cell Biology and Anatomy, Weill Medical
College of Cornell University, New York, New York 10012 and the
¶ Department of Human Genetics, Emory University, Atlanta,
Georgia 30322
*
This work was supported by a career development award, by
the Dolley Green Special Scholar Award (Research To Prevent Blindness), by The Foundation Fighting Blindness, and by National Institutes of
Health Grants EY11307 (to C.-H. S.), AG19206, and NS41449 (to X.-J. L.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Center of Molecular Biology, Air Force
General Hospital, Beijing 100036, China.
To whom correspondence should be addressed: The Margaret M. Dyson Vision Research Institute, Weill Medical College of Cornell University, 1300 York Ave., LC313, New York, NY 10021. Tel.:
212-746-2291; Fax: 212-746-6670; E-mail:
chsung@mail.med.cornell.edu.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  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]
|
|
|
|
 |
|
 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]
|
|
|
|
 |
|
 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]
|
|
|
|
 |
|
 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]
|
|
|
|
 |
|
 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]
|
|
|
|
|
|
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]
|
|
|
|
 |
|
 J. C. CROSS, D. G. SIMMONS, and E. D. WATSON Chorioallantoic Morphogenesis and Formation of the Placental Villous Tree Ann. N.Y. Acad. Sci., May 1, 2003; 995(1): 84 - 93. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 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 | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
