Title
Src-mediated tyrosine phosphorylation of dynamin is required for <tex>$\beta_{2}$</tex>-adrenergic receptor internalization and mitogen-activated protein kinase signaling Src-mediated tyrosine phosphorylation of dynamin is required for <tex>$\beta_{2}$</tex>-adrenergic receptor internalization and mitogen-activated protein kinase signaling
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences . Biomedical Sciences
Publication type
article
Publication
Baltimore, Md ,
Subject
Chemistry
Biology
Source (journal)
Journal of biological chemistry. - Baltimore, Md
Volume/pages
274(1999) :3 , p. 1185-1188
ISSN
0021-9258
ISI
000079956900002
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
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.
E-info
https://repository.uantwerpen.be/docman/iruaauth/795c86/9899081.pdf
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