Document Detail

Depletion of hsp90beta induces multiple defects in B cell receptor signaling.
MedLine Citation:
PMID:  16617057     Owner:  NLM     Status:  MEDLINE    
Hsp90 participates in many distinct aspects of cellular functions and accomplishes these roles by interacting with multiple client proteins. To gain insight into the interactions between Hsp90 and its clients, here we have reduced the protein level of Hsp90 in avian cells by gene targeting in an attempt to elicit the otherwise undetectable (because of the vast amount of cellular Hsp90) Hsp90-interacting proteins. Hsp90beta-deficient cells can grow, albeit more slowly than wild-type cells. B cell antigen receptor signaling is multiply impaired in these mutant cells; in particular, the amount of immunoglobulin M heavy chain protein is markedly reduced. Furthermore, serum activation does not promote ERK phosphorylation in Hsp90beta-deficient cells. These multifaceted depressive effects seem to be provoked independently of each other and possibly recapitulate the proteome-wide in vivo functions of Hsp90. Reintroduction of the Hsp90beta gene efficiently restores all of the defects. Unexpectedly, however, introducing the Hsp90alpha gene is also effective in restoration; thus, these defects might be caused by a reduction in the total expression of Hsp90 rather than by loss of Hsp90beta-specific function.
Fumika Shinozaki; Michiko Minami; Tomoki Chiba; Miho Suzuki; Katsuhiko Yoshimatsu; Yoshimasa Ichikawa; Kazuya Terasawa; Yasufumi Emori; Ken Matsumoto; Tomohiro Kurosaki; Akira Nakai; Keiji Tanaka; Yasufumi Minami
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-04-14
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  281     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2006 Jun 
Date Detail:
Created Date:  2006-06-12     Completed Date:  2006-08-01     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  16361-9     Citation Subset:  IM    
Department of Biophysics and Biochemistry, and Undergraduate Program for Bioinformatics and Systems Biology, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
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MeSH Terms
Cell Line
Extracellular Signal-Regulated MAP Kinases / metabolism
Gene Expression Regulation
HSP90 Heat-Shock Proteins / metabolism*
Hot Temperature
Plasmids / metabolism
Proteomics / methods
Receptors, Antigen, B-Cell / metabolism*
Signal Transduction
Reg. No./Substance:
0/HSP90 Heat-Shock Proteins; 0/Receptors, Antigen, B-Cell; EC Signal-Regulated MAP Kinases

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