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J Biol Chem, Vol. 275, Issue 8, 5591-5599, February 25, 2000
From the Department of Integrative Biology and Pharmacology,
University of Texas Health Sciences Center Houston,
Houston, Texas 77225
The sst2A receptor is expressed in the endocrine,
gastrointestinal, and neuronal systems as well as in many
hormone-sensitive tumors. This receptor is rapidly internalized and
phosphorylated in growth hormone-R2 pituitary cells following
somatostatin binding (Hipkin, R. W., Friedman, J., Clark, R. B., Eppler, C. M., and Schonbrunn, A. (1997) J. Biol.
Chem. 272, 13869-13876). The protein kinase C (PKC)
activator, phorbol 12-myristate 13-acetate (PMA), also stimulates sst2A
phosphorylation. Here we examine the mechanisms and
consequences of PMA and agonist-induced sst2A phosphorylation. Like
somatostatin, both PMA and bombesin increased sst2A receptor phosphorylation within 2 min. The PKC inhibitor GF109203X blocked PMA-
and bombesin- stimulated sst2A phosphorylation, whereas stimulation by the somatostatin analog SMS 201-995 was unaffected. Agonist and PMA
each stimulated phosphorylation in two receptor domains, the third
intracellular loop and the C-terminal tail. Functionally, PMA
dramatically increased the internalization of the sst2A receptor-ligand complex. This PMA stimulation was blocked by GF109203X, whereas basal
internalization was unaffected. However, neither basal nor PMA-stimulated internalization was altered by pertussis toxin, whereas
both were blocked by hypertonic sucrose. Therefore PKC activation and
agonist binding stimulate sst2A phosphorylation by distinct mechanisms,
and PKC potentiates internalization of the sst2A receptor via
clathrin-coated pits. Thus, hormonal stimulation of PKC-coupled
receptors may provide a mechanism for regulating the inhibitory actions
of somatostatin in target tissue.
Protein Kinase C Activation Stimulates the Phosphorylation
and Internalization of the sst2A Somatostatin Receptor*
,
*
This work was supported by Research Grant DK32234 (to
A. S.) from the NIDDK, National Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Partially supported by a postdoctoral fellowship from the Juvenile
Diabetes Foundation. Current address: Dept. of Immunology, Schering-Plough Research Inst., Kenilworth, NJ 07033-0539.
§
To whom correspondence should be addressed: Dept. of
Integrative Biology and Pharmacology, University of Texas Houston, P. O. Box 20708, Houston, TX 77225. Tel.: 713-500-7470; Fax:
713-500-7456; E-mail: aschonb@farmr1.med.uth.tmc.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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