You are here: Home :: Area NEM :: Life sciences :: Biochemistry

V.M. Longshaw, H.W. Dirr, G.L. Blatch, M. Lässle

The in Vitro Phosphorylation of the Co-Chaperone mSTI1 by Cell Cycle Kinases Substantiates a Predicted Casein Kinase II-p34cdc2-NLS (CcN) Motif

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 (p34^cdc2) at T¹⁹⁸, substantiating a predicted CKII-p34^cdc2-NLS (CcN) motif. The possible implications of this phosphorylation as a cell cycle checkpoint are discussed.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 381, 11/2000
Pages: 1133 - 1138

Show full article (external site)

Show all available items of this journal

 

Area NEM