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Originally published In Press as doi:10.1074/jbc.M011628200 on February 15, 2001

J. Biol. Chem., Vol. 276, Issue 19, 15939-15944, May 11, 2001
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Phosphorylation by cdc2-CyclinB1 Kinase Releases Cytoplasmic Dynein from Membranes*

Stephen G. Addinall, Petra S. Mayr, Sandra Doyle, John K. Sheehan, Philip G. Woodman, and Victoria J. AllanDagger

From the University of Manchester, School of Biological Sciences, Manchester, M13 9PT, United Kingdom

Movement of various cargoes toward microtubule minus ends is driven by the microtubule motor cytoplasmic dynein (CD). Many cargoes are motile only during certain cell cycle phases, suggesting that CD function may be under cell cycle control. Phosphorylation of the CD light intermediate chain (DLIC) has been suggested to play a crucial role in modulating CD function during the Xenopus embryonic cell cycle, where CD-driven organelle movement is active in interphase but greatly reduced in metaphase. This down-regulation correlates with hyperphosphorylation of DLIC and release of CD from the membrane. Here we investigate the role of the key mitotic kinase, cdc2-cyclinB1, in this process. We show that DLIC within the native Xenopus CD complex is an excellent substrate for purified Xenopus cdc2-glutathione S-transferase (GST) cyclinB1 (cdc2-GSTcyclinB1) kinase. Mass spectrometry of native DLIC revealed that a conserved cdc2 site (Ser-197) previously implicated in the metaphase modulation of CD remains phosphorylated in interphase and so is unlikely to be the key regulatory site. We also demonstrate that incubating interphase membranes with cdc2-GSTcyclinB1 kinase results in substantial release of CD from the membrane. These data suggest that phosphorylation of DLIC by cdc2 kinase leads directly to the loss of membrane-associated CD and an inhibition of organelle movement.

* This work was supported by Wellcome Trust Grant 048894/Z/96/A, Medical Research Council Co-operative Group Award G9722026, Medical Research Council Senior Fellowship G117/153 (to P. G. W.), and a Senior Fellowship from the Lister Institute of Preventive Medicine (to V. J. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF317841.

Dagger To whom correspondence should be addressed: University of Manchester, School of Biological Sciences, 2.205 Stopford Bldg., Oxford Rd., Manchester, M13 9PT, UK. Tel.: 44 161 275 5646; Fax: 44 161 275 5082; E-mail: viki.allan@man.ac.uk.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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