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Vol. 14, Issue 5, 1745-1756, May 2003
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* Department of Molecular Biology and Biochemistry, Rutgers University,
Piscataway, New Jersey 08855;
Department of Pharmacology, Kitasato University, Tokyo, Japan; and
Department of Pharmacology, Kyoto University, Kyoto, Japan
Submitted July 25, 2002;
Revised December 11, 2002;
Accepted January 30, 2003
Monitoring Editor: Tom Pollard
Citron kinase is a Rho-effector protein kinase that is related to Rho-associated kinases of ROCK/ROK/Rho-kinase family. Both ROCK and citron kinase are suggested to play a role in cytokinesis. However, no substrates are known for citron kinase. We found that citron kinase phosphorylated regulatory light chain (MLC) of myosin II at both Ser-19 and Thr-18 in vitro. Unlike ROCK, however, citron kinase did not phosphorylate the myosin binding subunit of myosin phosphatase, indicating that it does not inhibit myosin phosphatase. We found that the expression of the kinase domain of citron kinase resulted in an increase in MLC di-phosphorylation. Furthermore, the kinase domain was able to increase di-phosphorylation and restore stress fiber assembly even when ROCK was inhibited with a specific inhibitor, Y-27632. The expression of full-length citron kinase also increased di-phosphorylation during cytokinesis. These observations suggest that citron kinase phosphorylates MLC to generate di-phosphorylated MLC in vivo. Although both mono- and di-phosphorylated MLC were found in cleavage furrows, di-phosphorylated MLC showed more constrained localization than did mono-phosphorylated MLC. Because citron kinase is localized in cleavage furrows, citron kinase may be involved in regulating di-phosphorylation of MLC during cytokinesis.
Abbreviations used: MBS, myosin binding subunit or myosin targeting subunit of myosin phosphatase; MLC, regulatory light chain of myosin II; ROCK, Rho-associated kinase, Rho-kinase or ROK.
Corresponding authors. E-mail addresses:
yamashiro{at}mbcl.rutgers.edu;
matsumura{at}mbcl.rutgers.edu.
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