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The G-protein-coupled receptor phosphatase: a protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity.

dc.contributor.author Pitcher, JA
dc.contributor.author Payne, ES
dc.contributor.author Csortos, C
dc.contributor.author DePaoli-Roach, AA
dc.contributor.author Lefkowitz, RJ
dc.coverage.spatial United States
dc.date.accessioned 2013-09-10T15:50:43Z
dc.date.issued 1995-08-29
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/7667292
dc.identifier.issn 0027-8424
dc.identifier.uri https://hdl.handle.net/10161/7839
dc.description.abstract Phosphorylation of G-protein-coupled receptors plays an important role in regulating their function. In this study the G-protein-coupled receptor phosphatase (GRP) capable of dephosphorylating G-protein-coupled receptor kinase-phosphorylated receptors is described. The GRP activity of bovine brain is a latent oligomeric form of protein phosphatase type 2A (PP-2A) exclusively associated with the particulate fraction. GRP activity is observed only when assayed in the presence of protamine or when phosphatase-containing fractions are subjected to freeze/thaw treatment under reducing conditions. Consistent with its identification as a member of the PP-2A family, the GRP is potently inhibited by okadaic acid but not by I-2, the specific inhibitor of protein phosphatase type 1. Solubilization of the membrane-associated GRP followed by gel filtration in the absence of detergent yields a 150-kDa peak of latent receptor phosphatase activity. Western blot analysis of this phosphatase reveals a likely subunit composition of AB alpha C. PP-2A of this subunit composition has previously been characterized as a soluble enzyme, yet negligible soluble GRP activity was observed. The subcellular distribution and substrate specificity of the GRP suggests significant differences between it and previously characterized forms of PP-2A.
dc.language eng
dc.publisher Proceedings of the National Academy of Sciences
dc.relation.ispartof Proc Natl Acad Sci U S A
dc.subject Animals
dc.subject Blotting, Western
dc.subject Brain
dc.subject Cattle
dc.subject Cell Membrane
dc.subject Chromatography, Gel
dc.subject GTP-Binding Proteins
dc.subject Humans
dc.subject Phosphoprotein Phosphatases
dc.subject Receptor Protein-Tyrosine Kinases
dc.subject Receptors, Cell Surface
dc.subject Spodoptera
dc.subject Subcellular Fractions
dc.subject Substrate Specificity
dc.title The G-protein-coupled receptor phosphatase: a protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity.
dc.type Journal article
duke.contributor.id Lefkowitz, RJ|0096962
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/7667292
pubs.begin-page 8343
pubs.end-page 8347
pubs.issue 18
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 Institutes and Centers
pubs.organisational-group Medicine
pubs.organisational-group Medicine, Cardiology
pubs.organisational-group Pathology
pubs.organisational-group School of Medicine
pubs.organisational-group Trinity College of Arts & Sciences
pubs.publication-status Published
pubs.volume 92


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