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Multiple endocytic pathways of G protein-coupled receptors delineated by GIT1 sensitivity.

dc.contributor.author Achiriloaie, M
dc.contributor.author Albanesi, JP
dc.contributor.author Claing, A
dc.contributor.author Lefkowitz, Robert J
dc.contributor.author Perry, SJ
dc.contributor.author Premont, Richard Thomas
dc.contributor.author Walker, JK
dc.coverage.spatial United States
dc.date.accessioned 2013-09-05T17:48:57Z
dc.date.issued 2000-02-01
dc.identifier https://www.ncbi.nlm.nih.gov/pubmed/10655494
dc.identifier.issn 0027-8424
dc.identifier.uri http://hdl.handle.net/10161/7812
dc.description.abstract Recently, we identified a GTPase-activating protein for the ADP ribosylation factor family of small GTP-binding proteins that we call GIT1. This protein initially was identified as an interacting partner for the G protein-coupled receptor kinases, and its overexpression was found to affect signaling and internalization of the prototypical beta(2)-adrenergic receptor. Here, we report that GIT1 overexpression regulates internalization of numerous, but not all, G protein-coupled receptors. The specificity of the GIT1 effect is not related to the type of G protein to which a receptor couples, but rather to the endocytic route it uses. GIT1 only affects the function of G protein-coupled receptors that are internalized through the clathrin-coated pit pathway in a beta-arrestin- and dynamin-sensitive manner. Furthermore, the GIT1 effect is not limited to G protein-coupled receptors because overexpression of this protein also affects internalization of the epidermal growth factor receptor. However, constitutive agonist-independent internalization is not regulated by GIT1, because transferrin uptake is not affected by GIT1 overexpression. Thus, GIT1 is a protein involved in regulating the function of signaling receptors internalized through the clathrin pathway and can be used as a diagnostic tool for defining the endocytic pathway of a receptor.
dc.language eng
dc.relation.ispartof Proc Natl Acad Sci U S A
dc.subject Adaptor Proteins, Signal Transducing
dc.subject Animals
dc.subject COS Cells
dc.subject Cell Cycle Proteins
dc.subject Cells, Cultured
dc.subject Cercopithecus aethiops
dc.subject Cyclic AMP
dc.subject Endocytosis
dc.subject GTP-Binding Proteins
dc.subject GTPase-Activating Proteins
dc.subject Humans
dc.subject Phosphoproteins
dc.subject Receptor, Angiotensin, Type 1
dc.subject Receptor, Angiotensin, Type 2
dc.subject Receptor, Endothelin B
dc.subject Receptors, Adrenergic, beta
dc.subject Receptors, Angiotensin
dc.subject Receptors, Cell Surface
dc.subject Receptors, Endothelin
dc.subject Receptors, Muscarinic
dc.subject Receptors, Opioid, mu
dc.subject Receptors, Vasoactive Intestinal Peptide
dc.subject Recombinant Fusion Proteins
dc.subject Transfection
dc.title Multiple endocytic pathways of G protein-coupled receptors delineated by GIT1 sensitivity.
dc.type Journal article
pubs.author-url https://www.ncbi.nlm.nih.gov/pubmed/10655494
pubs.begin-page 1119
pubs.end-page 1124
pubs.issue 3
pubs.organisational-group Basic Science Departments
pubs.organisational-group Biochemistry
pubs.organisational-group Chemistry
pubs.organisational-group Clinical Science Departments
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Duke Institute for Brain Sciences
pubs.organisational-group Institutes and Centers
pubs.organisational-group Institutes and Provost's Academic Units
pubs.organisational-group Medicine
pubs.organisational-group Medicine, Cardiology
pubs.organisational-group Medicine, Gastroenterology
pubs.organisational-group Pathology
pubs.organisational-group School of Medicine
pubs.organisational-group School of Nursing
pubs.organisational-group Trinity College of Arts & Sciences
pubs.organisational-group University Institutes and Centers
pubs.publication-status Published
pubs.volume 97


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