Diverse signaling pathways in the cellular actions of insulin.
Saltiel, Alan R.
Department of Signal Transduction, Parke-Davis Pharmaceutical
Research, Division of Warner-Lambert Co., 2800 Plymouth Road, Ann
Arbor, Michigan 48105, ph: 313-996-3960, fax: 313-996-5668
APStracts 2:0223E, 1995.
Insulin is one of the most important regulators of glucose and lipid
homeostasis. Many of its cellular actions are mediated by changes in
protein phosphorylation. The consequences of these phosphorylation
events extend from a series of different short-term metabolic actions
to longer term effects of the hormone on cellular growth and
differentiation. While the insulin receptor itself is a tyrosine
kinase that is activated upon hormone binding, the ensuing changes in
phosphorylation occur predominantly on serine and threonine residues.
Moreover, insulin can simultaneously stimulate the phosphorylation of
some proteins, and the dephosphorylation of others. These paradoxical
effects of insulin suggest that separate signal transduction pathways
may emanate from the receptor itself, to produce the pleiotropic
actions of the hormone.
Received 31 May 1995; accepted in final form 27 October 1995.
APS Manuscript Number E239-5.
Article publication pending Am. J. Physiol. (Endocrinol. Metab.).
ISSN 1080-4757 Copyright 1995 The American Physiological Society.
Published in APStracts on 30 November 95