Publication
Title
Src-mediated tyrosine phosphorylation of dynamin is required for -adrenergic receptor internalization and mitogen-activated protein kinase signaling
Author
Abstract
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 beta(2)-adrenergic receptors (beta(2)-ARs) leads to c-Src-mediated tyrosine phosphorylation of dynamin, which is required for receptor internalization. Two tyrosine residues, Tyr(231) and Tyr(597), are identified as the major phosphorylation sites. Mutation of these residues to phenylalanine dramatically decreases the c-Src-mediated phosphorylation of dynamin following beta(2)-AR stimulation. Moreover, expression of Y231F/Y597F dynamin inhibits beta(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.
Language
English
Source (journal)
Journal of biological chemistry. - Baltimore, Md
Publication
Baltimore, Md : 1999
ISSN
0021-9258
Volume/pages
274:3(1999), p. 1185-1188
ISI
000079956900002
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Faculty/Department
Publication type
Subject
External links
Web of Science
Record
Identification
Creation 06.01.2015
Last edited 11.07.2017