beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis (Q28141212)

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scientific article (publication date: 14 April 2000)

Language	Label	Description	Also known as
English	beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis	scientific article (publication date: 14 April 2000)

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scholarly article

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beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis (English)

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Robert Lefkowitz

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object named as

R J Lefkowitz

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author name string

W E Miller

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S Maudsley

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S Ahn

3

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K D Khan

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L M Luttrell

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language of work or name

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publication date

14 April 2000

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Journal of Biological Chemistry

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275

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15

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11312-9

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G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization

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The pathways connecting G protein-coupled receptors to the nucleus through divergent mitogen-activated protein kinase cascades

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G-protein-coupled receptor regulation: role of G-protein-coupled receptor kinases and arrestins

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Endocytosis and recycling of G protein-coupled receptors

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Regulation of transmembrane signaling by receptor phosphorylation

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Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1

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Heptahelical receptor signaling: beyond the G protein paradigm.

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Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor

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Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain

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Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes

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Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation

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The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis

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Src: more than the sum of its parts

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Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel p130Cas-related protein, Sin.

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Role of c-Src tyrosine kinase in G protein-coupled receptor- and Gbetagamma subunit-mediated activation of mitogen-activated protein kinases

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G protein-coupled chemoattractant receptors regulate Lyn tyrosine kinase.Shc adapter protein signaling complexes

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Bombesin, bradykinin, vasopressin, and phorbol esters rapidly and transiently activate Src family tyrosine kinases in Swiss 3T3 cells. Dissociation from tyrosine phosphorylation of p125 focal adhesion kinase

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Switching of the coupling of the beta2-adrenergic receptor to different G proteins by protein kinase A.

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Signal characteristics of G protein-transactivated EGF receptor

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EGF receptor signaling stimulates SRC kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake.

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Src-mediated tyrosine phosphorylation of dynamin is required for beta2-adrenergic receptor internalization and mitogen-activated protein kinase signaling

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Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases

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Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands

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Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions

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Functional interaction between c-Src and its mitotic target, Sam 68

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A target for Src in mitosis.

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Association between src-kinases and the polyoma virus oncogene middle T-antigen requires PP2A and a specific sequence motif

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Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation

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Polyoma virus transforming protein associates with the product of the c-src cellular gene

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Src phosphorylates EAST, a novel EGF receptor-associated protein.

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Polyomavirus middle-T antigen associates with the kinase domain of Src-related tyrosine kinases.

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10.1074/JBC.275.15.11312

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