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

Longshaw, Victoria M and Dirr, Heini W and 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

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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.

Item Type: Article
Additional Information:

Online ISSN: 1437-4315

Uncontrolled Keywords: ResPubID22232. cell cycle kinases, heat shock protein, nuclear localisation, stress protein, proteins, murine, kinases
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 0601 Biochemistry and Cell Biology
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Depositing User: VUIR
Date Deposited: 13 Dec 2011 02:19
Last Modified: 23 Mar 2015 02:55
URI: http://vuir.vu.edu.au/id/eprint/8177
DOI: 10.1515/BC.2000.139
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Citations in Scopus: 20 - View on Scopus

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