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Blood, 15 December 2000, Vol. 96, No. 13, pp. 4236-4245
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Human CLP36, a PDZ-domain and LIM-domain protein, binds to
 -actinin-1 and associates with actin filaments and stress fibers
in activated platelets and endothelial cells
Kristin Bauer,
Michael Kratzer,
Marcus Otte,
Karin Luber de Quintana,
Jörg Hagmann,
Georg J. Arnold,
Christoph Eckerskorn,
Friedrich Lottspeich, and
Wolfgang Siess
From the Institut für Prophylaxe und
Epidemiologie der Kreislaufkrankheiten, München, Germany;
Genzentrum der Universität, München, Germany;
Friedrich-Miescher-Institut, Basel, Switzerland; Toplab GmbH,
Martinsried, Germany; and Max-Planck-Institut für Biochemie,
Martinsried, Germany.
A 38-kd protein that associates with F-actin structures in
activated platelets and endothelial cells was purified, cloned, and
characterized. The protein contains an N-terminal PDZ motif, a large
intervening sequence, and a C-terminal LIM domain and was identified as
the human homolog of rat CLP36. The study showed that CLP36 associates
with actin filaments and stress fibers that are formed during shape
change and spreading of platelets and during migration and contraction
of endothelial cells. CLP36 binds to  -actinin-1 as shown by
coimmunoprecipitation, pull-down experiments, yeast 2-hybrid analysis,
and blot overlay assays and colocalizes with -actinin-1 along
endothelial actin stress fibers. In contrast to -actinin-1, CLP36
was absent from focal adhesions in both activated platelets and
endothelial cells. The N-terminal part of CLP36 containing the PDZ
domain and the intervening region, but not the LIM domain, targeted
enhanced green fluorescent protein fusion proteins to stress fibers in
endothelial cells. Yeast 2-hybrid analysis demonstrated that the
intervening sequence, but not the PDZ or the LIM domain of CLP36, binds
to the spectrinlike repeats 2 and 3 of -actinin-1. The study further
shows that CLP36 binds to -actinin in resting platelets and
translocates as a CLP36/-actinin complex to the newly formed actin
cytoskeleton in activated platelets. The results indicate that CLP36
binds via -actinin-1 to actin filaments and stress fibers in
activated human platelets and endothelial cells. The study suggests
that CLP36 may direct -actinin-1 to specific actin structures and at
this position might modulate the function of -actinin-1.
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