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J Biol Chem, Vol. 273, Issue 37, 23633-23636, September 11, 1998
,,
From the Proteins of the p21-activated kinase (Pak) family
have been implicated in the regulation of gene expression, cytoskeletal architecture, and apoptosis. Although the ability of Cdc42 and Rac
GTPases to activate Pak is well established, relatively little else is
known about Pak regulation or the identity of Pak cellular targets.
Here we report the identification of two closely related Pak3-binding
proteins, possibly arising from alternative splicing, designated p50
and p85Cool-1 (cloned out
of library). Both isoforms of Cool contain a
Src homology 3 domain that directly mediates interaction with Pak3 and
tandem Dbl homology and pleckstrin homology domains. Despite the
presence of the Dbl homology-pleckstrin homology motif, a characteristic of Rho family activators, activation of Cdc42 or Rac by
Cool is not detectable. Instead binding of p50Cool-1, but
not p85Cool-1, to Pak3 represses its activation by upstream
activators such as the Dbl oncoprotein, indicating a novel mechanism of
regulation of Pak signaling.
Department of Molecular Medicine and the
§ Section of Biochemistry, Molecular and Cell Biology,
Cornell University, Ithaca, New York 14853-6401 and ¶ Cold Spring
Harbor Laboratory, Cold Spring Harbor, New York 11724
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