The in vitro phosphorylation of the co-chaperone mSTI1 by cell cycle kinases substantiates a predicted casein kinase II-p34(cdc2)-NLS(CcN) motif

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Longshaw, Victoria M, Dirr, Heini W, Blatch, Gregory L and Lässle, M (2000) The in vitro phosphorylation of the co-chaperone mSTI1 by cell cycle kinases substantiates a predicted casein kinase II-p34(cdc2)-NLS(CcN) motif. Biological Chemistry, 381 (11). pp. 1133-1138. ISSN 1431-6730

Abstract

The co-chaperone murine stress-inducible protein 1 (mSTI1), a Hsp70/Hsp90 organizing protein (Hop) homolog, functions as a physical link between Hsp70 and Hsp90 by mediating the formation of the mSTI1/ Hsp70/Hsp90 chaperone heterocomplex. We show here that mSTI1 is an in vitro substrate of cell cycle kinases. Casein kinase II (CKII) phosphorylates mSTI1 at S189, and cdc2 kinase (p34cdc2) at T198, substantiating a predicted CKII-p34cdc2-NLS (CcN) motif. The possible implications of this phosphorylation as a cell cycle checkpoint are discussed.

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Additional Information

Online ISSN: 1437-4315

Item type Article
URI https://vuir.vu.edu.au/id/eprint/8177
DOI https://doi.org/10.1515/BC.2000.139
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 0601 Biochemistry and Cell Biology
Keywords ResPubID22232. cell cycle kinases, heat shock protein, nuclear localisation, stress protein, proteins, murine, kinases
Citations in Scopus 25 - View on Scopus
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