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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1993-3-9
|
| pubmed:abstractText |
In order to determine which portion of phosphoinositide-specific phospholipase C (PLC)-beta 1 is required for activation by G alpha q, a series of specific deletions and truncations of PLC-beta 1 cDNA were prepared. After transfection of COS-7 cells with these cDNA clones, the activity and localization of the expressed proteins were determined. Specific deletions in the C-terminal end of the protein did not lead to loss of intrinsic enzymatic activity but did result in loss of the ability to be activated by G alpha q. The region required for activation was localized to the amino acid sequence corresponding to residues 903-1142 of PLC-beta 1. This region was further subdivided into two sequences; one extending from residues Thr-903 to Gln-1030 that was required for particulate fraction association as well as for activation by G alpha q and the other extending from residues Gln-1030 to Leu-1142 that was required for interaction with G alpha subunits. These results were confirmed by the observation that the C-terminal portion of PLC-beta 1, when co-expressed with the muscarinic acetylcholine receptor type 1 or the alpha 1C-adrenergic receptor in COS-7 cells, markedly inhibited ligand-induced release of inositol phosphates. In an in vitro system, two peptides derived from the G-protein interaction region at the C terminus were found to inhibit the guanosine 5'-3-O-(thio)triphosphate-dependent activation of PLC-beta 1 by G alpha q. This further localized the sites on PLC-beta 1 which are involved in interaction with G-protein alpha subunits.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carbachol,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Norepinephrine,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Muscarinic,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
268
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
3704-9
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:8381437-Amino Acid Sequence,
pubmed-meshheading:8381437-Animals,
pubmed-meshheading:8381437-Carbachol,
pubmed-meshheading:8381437-Cell Line,
pubmed-meshheading:8381437-Cloning, Molecular,
pubmed-meshheading:8381437-Enzyme Activation,
pubmed-meshheading:8381437-GTP-Binding Proteins,
pubmed-meshheading:8381437-Inositol Phosphates,
pubmed-meshheading:8381437-Kinetics,
pubmed-meshheading:8381437-Molecular Sequence Data,
pubmed-meshheading:8381437-Mutagenesis,
pubmed-meshheading:8381437-Norepinephrine,
pubmed-meshheading:8381437-Phosphatidylinositol Diacylglycerol-Lyase,
pubmed-meshheading:8381437-Phosphoric Diester Hydrolases,
pubmed-meshheading:8381437-Plasmids,
pubmed-meshheading:8381437-Receptors, Muscarinic,
pubmed-meshheading:8381437-Recombinant Proteins,
pubmed-meshheading:8381437-Restriction Mapping,
pubmed-meshheading:8381437-Sequence Deletion,
pubmed-meshheading:8381437-Transfection
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Identification of critical regions on phospholipase C-beta 1 required for activation by G-proteins.
|
| pubmed:affiliation |
Division of Biology, California Institute of Technology, Pasadena 91125.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|