Depletion of Hsp90β Induces Multiple Defects in B Cell Receptor Signaling
| Autor: | Yasufumi Emori, Akira Nakai, Tomohiro Kurosaki, Kazuya Terasawa, Ken Matsumoto, Yasufumi Minami, Katsuhiko Yoshimatsu, Fumika Shinozaki, Miho Suzuki, Keiji Tanaka, Yoshimasa Ichikawa, Michiko Minami, Tomoki Chiba |
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| Rok vydání: | 2006 |
| Předmět: |
Proteomics
Hot Temperature B-cell receptor Receptors Antigen B-Cell Biology Transfection Biochemistry Cell Line In vivo Animals HSP90 Heat-Shock Proteins Extracellular Signal-Regulated MAP Kinases Molecular Biology Gene Gene targeting Cell Biology Molecular biology Hsp90 B cell receptor signaling Cell biology Gene Expression Regulation Immunoglobulin M biology.protein Chickens Function (biology) Plasmids Signal Transduction |
| Zdroj: | Journal of Biological Chemistry. 281:16361-16369 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m600891200 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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