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Vol. 54, Issue 6, 935-941, December 1998
Endocrinology and Reproduction Research Branch, National
Institute of Child Health and Human Development, National Institutes of
Health, Bethesda, Maryland 20892 (R.D.S., J.A.O-R., S.J., K.J.C.), and
Department of Physiology, Semmelweis University of Medicine, H-1088,
Budapest, Hungary (L.H., B.M.)
The agonist-induced phosphorylation sites of the rat AT1a
angiotensin receptor were analyzed using epitope-tagged mutant
receptors expressed in Cos-7 cells. Angiotensin II-stimulated receptor
phosphorylation was unaffected by truncation of the cytoplasmic tail of
the receptor at Ser342 (
342) but was abolished by truncation at
Ser325 (325). Truncation at Ser335 (335), or double-point
mutations of Ser335 and Thr336 to alanine (ST-AA), reduced receptor
phosphorylation by ~50%, indicating that in addition to Ser335
and/or Thr336, amino acids within the Ser326-Thr332 segment are also
phosphorylated. Agonist-induced phosphorylation of the ST-AA and 335
receptors was partially inhibited by staurosporine, suggesting that the single protein kinase C consensus site in the Ser326-Thr332 segment (Ser331) is phosphorylated. The impairment of receptor phosphorylation was broadly correlated with the attenuation of agonist-induced internalization rates (325 < 335 < ST-AA < 342 < wild-type) and with the increasing rank order of
magnitude of inositol phosphate production normalized to an equal
number of receptors (325 > 335 > ST-AA = 342 > wild-type). These results demonstrate that agonist-induced phosphorylation of the AT1a receptor is
confined to an 11-amino-acid serine/threonine-rich segment of its
carboxyl-terminal cytoplasmic tail and implicate this region in the
mechanisms of receptor internalization and desensitization.
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