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J. Biol. Chem., Vol. 276, Issue 24, 21841-21848, June 15, 2001
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From the We have recently identified and cloned a novel
member of mitogen-activated protein kinase superfamily protein,
MOK (Miyata, Y., Akashi, M., and Nishida, E. (1999) Genes
Cells 4, 299-309). To address its regulatory mechanisms, we
searched for cellular proteins that specifically associate with MOK by
co-immunoprecipitation experiments. Several cellular proteins including
a major 90-kDa molecular chaperone HSP90 were found associated with
MOK. Treatment of cells with geldanamycin, an HSP90-specific inhibitor,
rapidly decreased the protein level of MOK, and the decrease was
attributed to enhanced degradation of MOK through
proteasome-dependent pathways. Our data suggest that the
association with HSP90 may regulate intracellular protein stability and
solubility of MOK. Experiments with a series of deletion mutants of MOK
indicated that the region encompassing the protein kinase catalytic
subdomains I-IV is required for HSP90 binding. Closely related protein
kinases (male germ cell-associated kinase and male germ cell-associated
kinase-related kinase) were also found to associate with HSP90, whereas
conventional mitogen-activated protein kinases (extracellular
signal-regulated kinase, p38, and c-Jun N-terminal
kinase/stress-activated protein kinase) were not associated with HSP90.
In addition, we found that other molecular chaperones including Cdc37,
HSC70, HSP70, and HSP60 but not GRP94, FKBP52, or Hop were detected
specifically in the MOK-HSP90 immunocomplexes. These results taken
together suggest a role of a specific set of molecular chaperones in
the stability of signal-transducing protein kinases.
Specific Association of a Set of Molecular Chaperones Including
HSP90 and Cdc37 with MOK, a Member of the Mitogen-activated
Protein Kinase Superfamily*
§,
, and
Department of Cell and Developmental
Biology, Graduate School of Biostudies, Kyoto University, Kitashirakawa
Oiwake-cho, Sakyo-ku, Kyoto 606-8502, Japan, the ¶ Department of
Retroviral Regulation, Tokyo Medical and Dental University, Medical
Research Division, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8519, Japan,
and the Department of Genetics, Institute of Medical Science,
University of Tokyo, Minato-ku, Tokyo 108-8639, Japan
*
This work was supported by grants-in-aid for scientific
research (to Y. M. and E. N.) from the Ministry of Education,
Science, and Culture of Japan.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.
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