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(Received for publication, March 28, 1997, and in revised form, July 9, 1997)
From INSERM Unité 151, Institut Louis Bugnard, CHU Rangueil,
F 31403 Toulouse Cedex, France, Activation of the somatostatin receptor sst2, a
member of the Gi protein-coupled receptor family,
results in the stimulation of a protein-tyrosine phosphatase activity
involved in the sst2-mediated growth inhibitory signal. Here, we report
that SHP-1, a cytoplasmic protein-tyrosine phosphatase containing two
Src homology 2 domains constitutively associated with sst2 as evidence
by coprecipitation of SHP-1 protein with sst2, in Chinese hamster ovary
cells coexpressing sst2 and SHP-1. Activation of sst2 by somatostatin
resulted in a rapid dissociation of SHP-1 from sst2 accompanied by an
increase of SHP-1 activity. SHP-1 was phosphorylated on tyrosine in
control cells and somatostatin induced a rapid and transient
dephosphorylation on tyrosine residues of the enzyme. Stimulation of
SHP-1 activity by somatostatin was abolished by pertussis toxin
pretreatment of cells. Gi
Volume 272, Number 39,
Issue of September 26, 1997
pp. 24448-24454
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Laboratoire de
Génétique et Physiologie du développement, Luminy
CASE 907, 13288 Marseille Cedex 9, France, and § Institut
Cochin de Génétique Moléculaire, 75014 Paris, France
3 was specifically
immunoprecipitated by anti-sst2 and anti-SHP-1 antibodies, and
somatostatin induced a rapid dissociation of Gi3 from
sst2, suggesting that Gi3 may be involved in the
sst2·SHP-1 complexes. Finally, somatostatin inhibited the proliferation of cells coexpressing sst2 and SHP-1, and this effect was
suppressed in cells coexpressing sst2 and the catalytic inactive SHP-1
(C453S mutant). Our data identify SHP-1 as the tyrosine phosphatase
associated with sst2 and demonstrate that this enzyme may be an initial
key transducer of the antimitogenic signaling mediated by sst2.
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