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(Received for publication, June 20, 1996, and in revised form, September 16, 1996)
From the The NCK adapter protein is comprised of three
consecutive Src homology 3 (SH3) protein-protein interaction domains
and a C-terminal SH2 domain. Although the association of NCK with
activated receptor protein-tyrosine kinases, via its SH2 domain,
implicates NCK as a mediator of growth factor-induced signal
transduction, little is known about the pathway(s) downstream of NCK
recruitment. To identify potential downstream effectors of NCK we
screened a bacterial expression library to isolate proteins that bind
its SH3 domains. Two molecules were isolated, the Wiskott-Aldrich
syndrome protein (WASP, a putative CDC42 effector) and a
serine/threonine protein kinase (PRK2, closely related to the putative
Rho effector PKN). Using interspecific backcross analysis the
Prk2 gene was mapped to mouse chromosome 3. Unlike WASP,
which bound the SH3 domains of several signaling proteins, PRK2
specifically bound to the middle SH3 domain of NCK and (weakly) that of
phospholipase C
Volume 271, Number 46,
Issue of November 15, 1996
pp. 28772-28776
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
Department of Biochemistry and Molecular
Biology and the Walther Oncology Center, Indiana University School of
Medicine, Indianapolis, Indiana 46202, Departments of
¶ Pharmacology and ** Biology and the
Lineberger Comprehensive Cancer Center,
University of North Carolina, Chapel Hill, North Carolina 27599, and
§§ Mammalian Genetics Laboratory, ABL Basic
Research Program, NCI-Frederick Cancer Research and Development Center,
Frederick, Maryland 21702
. PRK2 also specifically bound to Rho in a
GTP-dependent manner and cooperated with Rho family
proteins to induce transcriptional activation via the serum response
factor. These data suggest that PRK2 may coordinately mediate signal
transduction from activated receptor protein-tyrosine kinases and Rho
and that NCK may function as an adapter to connect receptor-mediated
events to Rho protein signaling.
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