Gastrointestinal peptide signaling through tyrosine phosphorylation
of focal adhesion proteins.
Rozengurt, Enrique.
Department of Medicine, Division of Digestive Diseases, School of
Medicine and Molecular Biology Institute, University of California,
Los Angeles, CA.90095
APStracts 5:0140G, 1998.
Gastrointestinal (GI) peptides (also referred to as neuropeptides or
regulatory peptides), including mammalian bombesin-like peptides,
gastrin and cholecystokinin (CCK), elicit the synthesis of classic
second messengers (e.g.,Ca2+, diacylglycerol, cAMP) and the
consequent stimulation of serine/threonine protein kinase cascades.
An emerging theme in signal transduction is that these agonists also
induce rapid and coordinate tyrosine phosphorylation of a set of
focal adhesion proteins including the non-receptor tyrosine kinase
p125fak and the adaptor proteins p130cas and paxillin. GI peptide
-mediated induction of tyrosine phosphorylation of these focal
adhesion proteins is critically dependent on the integrity of the
actin cytoskeleton and on functional Rho. The purpose of this article
is to review recent advances in unraveling this novel tyrosine kinase
pathway(s) because it appears to play a fundamental role in the
mediation of important biologic effects induced by GI peptides
including cell migration and proliferation.
Received 18 May 1998; accepted in final form 18 May 1998.
APS Manuscript Number G204-8.
Article publication pending Am. J. Physiol. (Gastrointest. Liver
Physiology).
ISSN 1080-4757 Copyright 1998 The American Physiological Society.
Published in APStracts on 16 June 1998