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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2017: 3.022

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 381, Issue 11


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

V.M. Longshaw / H.W. Dirr / G.L. Blatch / M. Lässle
Published Online: 2005-07-05 | DOI: https://doi.org/10.1515/BC.2000.139


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.

About the article

Published Online: 2005-07-05

Published in Print: 2000-11-15

Citation Information: Biological Chemistry, Volume 381, Issue 11, Pages 1133–1138, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2000.139.

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