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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 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 cycle checkpoint are discussed.

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