rdf:type |
|
lifeskim:mentions |
umls-concept:C0010222,
umls-concept:C0043393,
umls-concept:C0066772,
umls-concept:C0871261,
umls-concept:C1154588,
umls-concept:C1414254,
umls-concept:C1704259,
umls-concept:C1704632,
umls-concept:C1705987,
umls-concept:C1706817,
umls-concept:C1823197,
umls-concept:C2911692
|
pubmed:issue |
3
|
pubmed:dateCreated |
1998-2-12
|
pubmed:abstractText |
We have functionally expressed the human cDNA encoding the putative lysophosphatidic acid (LPA) receptor Edg-2 (Vzg-1) in Saccharomyces cerevisiae in an attempt to determine the agonist specificity of this G-protein-coupled receptor. LPA activated the pheromone response pathway in S. cerevisiae expressing Edg-2 in a time- and dose-dependent manner as determined by induction of a pheromone-responsive FUS1::lacZ reporter gene. LPA-mediated activation of the pheromone response pathway was dependent on mutational inactivation of the SST2 gene, the GTPase-activating protein for the yeast G alpha protein (the GPA1 gene product). This indicates that, in sst2 delta yeast cells, Edg-2 can efficiently couple to the yeast heterotrimeric G-protein in response to LPA and activate the yeast mitogen-activated protein kinase pathway. The Edg-2 receptor showed a high degree of specificity for LPA; other lyso-glycerophospholipids, sphingosine 1-phosphate, and diacyl-glycerophospholipids did not activate FUS1::lacZ. LPA analogs including a cyclic phosphoester form and ether-linked forms of LPA activated FUS1::lacZ, although fatty acid chains of 6 and 10 carbons did not activate FUS1::lacZ, suggesting a role for the side chain in ligand binding or receptor activation. These results indicate that Edg-2 encodes a highly specific LPA receptor.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lysophospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/MFA2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Pheromones,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lysophosphatidic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
16
|
pubmed:volume |
273
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1506-10
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pubmed:dateRevised |
2008-10-23
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pubmed:meshHeading |
pubmed-meshheading:9430689-Dose-Response Relationship, Drug,
pubmed-meshheading:9430689-Fungal Proteins,
pubmed-meshheading:9430689-GTP-Binding Proteins,
pubmed-meshheading:9430689-Humans,
pubmed-meshheading:9430689-Lipoproteins,
pubmed-meshheading:9430689-Lysophospholipids,
pubmed-meshheading:9430689-Pheromones,
pubmed-meshheading:9430689-Protein Binding,
pubmed-meshheading:9430689-Protein Conformation,
pubmed-meshheading:9430689-Receptors, Cell Surface,
pubmed-meshheading:9430689-Receptors, G-Protein-Coupled,
pubmed-meshheading:9430689-Receptors, Lysophosphatidic Acid,
pubmed-meshheading:9430689-Saccharomyces cerevisiae,
pubmed-meshheading:9430689-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9430689-Time Factors
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pubmed:year |
1998
|
pubmed:articleTitle |
Edg-2/Vzg-1 couples to the yeast pheromone response pathway selectively in response to lysophosphatidic acid.
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pubmed:affiliation |
LXR Biotechnology Inc., Richmond, California 94804, USA. jerickson@lxr.com
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pubmed:publicationType |
Journal Article
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