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Stress-inducible, murine protein mSTI1: Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases

Lässle, M and Blatch, Gregory L and Kundra, V and Takatori, T and Zetter, B (1997) Stress-inducible, murine protein mSTI1: Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases. Tthe Journal of Biological Chemistry, 272 (3). pp. 1876-1884. ISSN 0021-9258

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Abstract

We have recently isolated the cDNA for the murine homologue of the stress-inducible phosphoprotein STI1 (also known as IEF SSP 3521 or p60). STI1 was previously shown to be 2-fold up-regulated in MRC-5 fibroblasts upon viral transformation and to exist in a macromolecular complex with heat shock proteins of the HSP 70 and 90 families. By peptide-sequencing we have identified the two heat shock proteins that bind to murine STI1 (mSTI1) as HSC 70 and HSP 84/86. We describe two separate binding regions within mSTI1 for the two heat shock proteins. In the presence of cell extracts, the N-terminal region of mSTI1 binds preferentially to HSC 70, whereas the C-terminal portion of the molecule promotes the binding of HSP 84/86. Heat treatment caused a strong induction of mSTI1 message without affecting the steady-state level of the protein significantly. In addition, heat treatment led to changes in the isoformcomposition of mSTI1. pp70s6k, pp90rsk, and mitogenactivated protein kinase-activated protein kinase 2 were tested as possible STI1 kinases in vitro using recombinant mSTI1 as a substrate: only pp90rsk was able to phosphorylate recombinant mSTI1. In vitro kinase assays using casein kinase II suggest serine 189 to be a likely phosphorylation site in mSTI1.

Item Type: Article
Uncontrolled Keywords: ResPubID22237. mice, murine proteins, mSTI1, molecular binding, heat treatment, cDNA, DNA, in vitro phosphorylation, kinases
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 0601 Biochemistry and Cell Biology
FOR Classification > 0604 Genetics
Depositing User: VUIR
Date Deposited: 13 Dec 2011 00:37
Last Modified: 13 Dec 2011 00:37
URI: http://vuir.vu.edu.au/id/eprint/8182
DOI: 10.1074/jbc.272.3.1876
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Citations in Scopus: 107 - View on Scopus

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