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Research Article |
Haartman Institute and Helsinki University Central Hospital, Biomedicum Helsinki, P.O. Box 63, 00014 University of Helsinki, Finland
* Author for correspondence (e-mail: tomi.makela{at}helsinki.fi )
Accepted 6 March 2002
In this report we have characterized a novel, ubiquitously expressed
kinase, Clik1, that is predominantly nuclear and undergoes
autophosphorylation. Yeast two-hybrid analysis indicated a highly specific
association between Clik1 and CLP-36, which was identified in 36 out of 37
Clik1-interacting clones. CLP-36 is a PDZ-LIM protein that localizes to actin
stress fibers in nonmuscle cells and associates with
-actinin via its
PDZ-domain. The association of CLP-36 with Clik1, in turn, is mediated by the
C-terminal part of CLP-36 containing the LIM domain, and association was not
noted with the closely related ALP PDZ-LIM protein. Interestingly, the
association with CLP-36 led to relocalization of the otherwise nuclear Clik1
kinase to actin stress fibers, where it disrupted the periodic staining
pattern of CLP-36. Taken together these results establish the CLP-36 PDZ-LIM
protein as an adapter, recruiting the Clik1 kinase to actin stress fibers in
nonmuscle cells, and suggest that Clik1 represents a novel regulator of actin
stress fibers.
Key words: PDZ, LIM, Stress fibers, Kinase
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