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

Authors
Longshaw, VM Dirr, HW Blatch, GL Lassle, M
Citation
Vm. Longshaw et al., The in vitro phosphorylation of the co-chaperone mSTI1 by cell cycle kinases substantiates a predicted casein kinase II-p34(cdc2)-NLS (CcN) motif, BIOL CHEM, 381(11), 2000, pp. 1133-1138
Citations number
41
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOLOGICAL CHEMISTRY
ISSN journal
14316730 → ACNP
Volume
381
Issue
11
Year of publication
2000
Pages
1133 - 1138
Database
ISI
SICI code
1431-6730(200011)381:11<1133:TIVPOT>2.0.ZU;2-U
Abstract
The co-chaperone murine stress-inducible protein 1 (mSTI1), a Hsp70/Hsp90 o rganizing protein (Hop) homolog, functions as a physical link between Hsp70 and Hsp90 by mediating the formation of the mSTI1/ Hsp70/Hsp90 chaperone h eterocomplex. We show here that mSTI1 is an in vitro substrate of cell cycl e kinases. Casein kinase II (CKII) phosphorylates mSTI1 at S-189, and cdc2 kinase (p34(cdc2)) at T-198, substantiating a predicted CKII-p34(cdc2)-NLS (CcN) motif. The possible implications of this phosphorylation as a cell cy cle checkpoint are discussed.