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

Download

Full text for this resource is not available from the Research Repository.

Export

Longshaw, Victoria M, Dirr, Heini W, Blatch, Gregory ORCID: 0000-0003-0778-8577 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.

Dimensions Badge

Altmetric Badge

Additional Information	Online ISSN: 1437-4315
Item type	Article
URI	https://vuir.vu.edu.au/id/eprint/8177
DOI	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	27 - View on Scopus
Download/View statistics	View download statistics for this item