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J. Biol. Chem., Vol. 277, Issue 24, 22093-22102, June 14, 2002
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From the Department of Biomolecular Sciences, Graduate School of
Life Sciences, Tohoku University, Sendai, Miagi 980-8578, Japan
Actin filament dynamics play a critical
role in mitosis and cytokinesis. LIM motif-containing protein kinase 1 (LIMK1) regulates actin reorganization by phosphorylating and
inactivating cofilin, an actin-depolymerizing and -severing protein. To
examine the role of LIMK1 and cofilin during the cell cycle, we
measured cell cycle-associated changes in the kinase activity of LIMK1
and in the level of cofilin phosphorylation. Using synchronized HeLa cells, we found that LIMK1 became hyperphosphorylated and activated in
prometaphase and metaphase, then gradually returned to the basal level
as cells entered into telophase and cytokinesis. Although Rho-associated kinase and p21-activated protein kinase
phosphorylate and activate LIMK1, they are not likely to be involved in
mitosis-specific activation and phosphorylation of LIMK1. Immunoblot
and immunofluorescence analyses using an anti-phosphocofilin-specific
antibody revealed that the level of cofilin phosphorylation, similar to
levels of LIMK1 activity, increased during prometaphase and metaphase
then gradually declined in telophase and cytokinesis. Ectopic
expression of LIMK1 increased the level of cofilin phosphorylation
throughout the cell cycle and induced the formation of multinucleate
cells. These results suggest that LIMK1 is involved principally in
control of mitosis-specific cofilin phosphorylation and that
dephosphorylation and reactivation of cofilin at later stages of
mitosis play a critical role in cytokinesis of mammalian cells.
Mitosis-specific Activation of LIM Motif-containing Protein
Kinase and Roles of Cofilin Phosphorylation and
Dephosphorylation in Mitosis*
*
This work was supported by a grant-in-aid for creative
scientific research from the Japan Society of the Promotion of Science and a grant-in-aid for scientific research from the Ministry of Education, Science, Technology, Sports, and Culture of Japan.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.
To whom correspondence should be addressed: Dept. of
Biomolecular Sciences, Graduate School of Life Sciences, Tohoku
University, Aramaki-aza-Aoba, Aoba-ku, Sendai, Miagi 980-8578, Japan. Tel.: 81-22-217-6676; Fax: 81-22-217-6678; E-mail:
kmizuno@biology.tohoku.ac.jp.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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