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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
1995-10-12
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-1325671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-1325672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-1328247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-14731592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-1658556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-1664548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2157202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2159327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2165947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2540796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2549856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2550422,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2550453,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2558719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2827745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2837466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2837763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-2842604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-3032961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-4545509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-6094963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-6204887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-7681598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-7744811,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-7918404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-7925460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-8051102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-8133283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-8170959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-8288648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-8294450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-8380158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-8389371,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7667292-8394172
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
92
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8343-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7667292-Animals,
pubmed-meshheading:7667292-Blotting, Western,
pubmed-meshheading:7667292-Brain,
pubmed-meshheading:7667292-Cattle,
pubmed-meshheading:7667292-Cell Membrane,
pubmed-meshheading:7667292-Chromatography, Gel,
pubmed-meshheading:7667292-GTP-Binding Proteins,
pubmed-meshheading:7667292-Humans,
pubmed-meshheading:7667292-Phosphoprotein Phosphatases,
pubmed-meshheading:7667292-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:7667292-Receptors, Cell Surface,
pubmed-meshheading:7667292-Spodoptera,
pubmed-meshheading:7667292-Subcellular Fractions,
pubmed-meshheading:7667292-Substrate Specificity
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pubmed:year |
1995
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pubmed:articleTitle |
The G-protein-coupled receptor phosphatase: a protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity.
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pubmed:affiliation |
Howard Hughes Medical Research Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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