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(Received for publication, April 16, 1996, and in revised form, June 30, 1997)
From the Department of Pharmacology, Cornell University, Ithaca,
New York 14853-6401
Cdc42 plays an important role in intracellular
signaling pathways that influence cell morphology and motility and
stimulate DNA synthesis. In attempts to determine whether nonreceptor
tyrosine kinases play a fundamental role in Cdc42 signaling, we have
cloned and biochemically characterized a new Cdc42-associated tyrosine kinase (ACK) from bovine brain. This tyrosine kinase, named ACK-2, has
a calculated molecular mass of 83 kDa and shares a number of primary
structural domains with the 120-kDa ACK (ACK-1). The main differences
between the primary structures of ACK-2 and ACK-1 occur in the amino-
and carboxyl-terminal regions. Like ACK-1, ACK-2 binds exclusively to
activated (GTP-bound) Cdc42 and does not bind to its closest homologs,
e.g. activated Rac. ACK-2 could not be activated by
addition of glutathione S-transferase (GST)-Cdc42(Q61L), a
GTPase-defective mutant, or by GTP
Volume 272, Number 40,
Issue of October 3, 1997
pp. 24819-24824
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
S-loaded GST-Cdc42 in in vitro kinase assays. However, ACK-2 was activated when
cotransfected with wild type Cdc42 or Cdc42(Q61L) and stably associated
with Cdc42(Q61L) in vivo, indicating that ACK-2 interacts
with active Cdc42 in cells. Furthermore, the tyrosine kinase activity
of ACK-2 was stimulated both by epidermal growth factor and bradykinin, suggesting that ACK-2 may play a role in the signaling actions of both
receptor tyrosine kinases or heterotrimeric G-protein-coupled receptors.
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