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J Biol Chem, Vol. 274, Issue 3, 1185-1188, January 15, 1999
2-Adrenergic Receptor Internalization and
Mitogen-activated Protein Kinase Signaling
§,,¶, and
From the Some forms of G protein-coupled receptor
signaling, such as activation of mitogen-activated protein kinase
cascade as well as resensitization of receptors after hormone-induced
desensitization, require receptor internalization via
dynamin-dependent clathrin-coated pit mechanisms. Here we
demonstrate that activation of Howard Hughes Medical Institute and the
Departments of § Pharmacology and Cancer Biology,
¶ Medicine, and ** Surgery, Duke University Medical Center,
Durham, North Carolina 27710
2-adrenergic receptors (2-ARs) leads to c-Src-mediated tyrosine
phosphorylation of dynamin, which is required for receptor
internalization. Two tyrosine residues, Tyr231 and
Tyr597, are identified as the major phosphorylation sites.
Mutation of these residues to phenylalanine dramatically decreases the c-Src-mediated phosphorylation of dynamin following 2-AR
stimulation. Moreover, expression of Y231F/Y597F dynamin inhibits
2-AR internalization and the isoproterenol-stimulated
mitogen-activated protein kinase activation. Thus, agonist-induced,
c-Src-mediated tyrosine phosphorylation of dynamin is essential for its
function in clathrin mediated G protein-coupled receptor endocytosis.
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