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Vol. 12, Issue 4, 1131-1145, April 2001
*Biological Institute, Graduate School of Science, Tohoku
University, Sendai 980-8578, Japan; Testicular protein kinase 1 (TESK1) is a serine/threonine kinase
with a structure composed of a kinase domain related to those of
LIM-kinases and a unique C-terminal proline-rich domain. Like LIM-kinases, TESK1 phosphorylated cofilin specifically at Ser-3, both
in vitro and in vivo. When expressed in HeLa cells, TESK1 stimulated
the formation of actin stress fibers and focal adhesions. In contrast
to LIM-kinases, the kinase activity of TESK1 was not enhanced by
Rho-associated kinase (ROCK) or p21-activated kinase, indicating that
TESK1 is not their downstream effector. Both the kinase activity of
TESK1 and the level of cofilin phosphorylation increased by plating
cells on fibronectin. Y-27632, a specific inhibitor of ROCK, inhibited
LIM-kinase-induced cofilin phosphorylation but did not affect
fibronectin-induced or TESK1-induced cofilin phosphorylation in HeLa
cells. Expression of a kinase-negative TESK1 suppressed cofilin
phosphorylation and formation of stress fibers and focal adhesions
induced in cells plated on fibronectin. These results suggest that
TESK1 functions downstream of integrins and plays a key role in
integrin-mediated actin reorganization, presumably through
phosphorylating and inactivating cofilin. We propose that TESK1 and
LIM-kinases commonly phosphorylate cofilin but are regulated in
different ways and play distinct roles in actin reorganization in
living cells.
Department of
Biology, Kyushu University Graduate School of Science, Fukuoka
812-8581, Japan; and §Department of Pharmacology, Kyoto
University Faculty of Medicine, Kyoto 606-8315, Japan
Present address: Department of Cell
Biology, The Scripps Research Institute, 10550 North Torrey Pines Road,
La Jolla, CA 92037.
Corresponding author. E-mail address:
kmizuno{at}biology.tohoku.ac.jp.
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