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The in Vitro Phosphorylation of the Co-Chaperone mSTI1 by Cell Cycle Kinases Substantiates a Predicted Casein Kinase II-p34cdc2-NLS (CcN) Motif
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V.M. Longshaw
, H.W. Dirr , G.L. Blatch and M. Lässle
Published/Copyright:
July 5, 2005
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.
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Published Online: 2005-07-05
Published in Print: 2000-11-15
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Purification and Cloning of Type A/B hnRNP Proteins Involved in Transcriptional Activation from the Rat spi 2 Gene GAGA Box
- Release of Ribosome-Bound 5S rRNA upon Cleavage of the Phosphodiester Bond between Nucleotides A54 and A55 in 5S rRNA
- Noncovalent Binding of Poly(ADP-Ribose) to Nuclear Matrix Proteins: Developmental Changes and Tissue Specificity
- Mutational Analysis of Two PWW Sequence Motifs in Human Aminoacylase 1
- Divergent Enzyme Kinetics and Structural Properties of the Two Human Mitochondrial Creatine Kinase Isoenzymes
- Cloning, Heterologous Expression and Kinetic Analysis of Glycerol Kinase (TbGLK1) from Trypanosoma brucei
- Identification of the 50S Ribosomal Proteins from the Eubacterium Thermus thermophilus
- The Hyper-Thermostable Fe-Superoxide Dismutase from the Archaeon Acidianus ambivalens: Characterization, Recombinant Expression, Crystallization and Effects of Metal Exchange
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