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rdf:type |
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lifeskim:mentions |
umls-concept:C0014834,
umls-concept:C0017262,
umls-concept:C0033414,
umls-concept:C0068635,
umls-concept:C0205245,
umls-concept:C0243192,
umls-concept:C0599220,
umls-concept:C1167622,
umls-concept:C1171362,
umls-concept:C1515670,
umls-concept:C1948027
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pubmed:issue |
2-3
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pubmed:dateCreated |
2001-4-5
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pubmed:abstractText |
To analyze the coupling of Galpha subunits to the rat neurotensin receptor NTS-1 (NTR), fusion proteins were expressed in Escherichia coli with various Galpha subunits covalently linked to the receptor C-terminus. The presence of Galpha(q) or Galpha(i/q), in which the six C-terminal residues of Galpha(i1) were replaced with those from Galpha(q), increased the percentage of receptors in the agonist high-affinity state. This effect was less pronounced for wild-type Galpha(i1) and not observed for Galpha(i/s). Functional coupling of neurotensin receptor to Galpha was demonstrated by neurotensin-induced [(35)S]GTPgammaS binding for the Galpha(q), Galpha(i/q) and Galpha(i1) subunits, but not for Galpha(i/s). Our results extend previous findings of the dual coupling of NTR to pertussis toxin-sensitive and -insensitive G-proteins in Chinese hamster ovary cells with preference for the latter.
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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 |
Mar
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
493
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
101-5
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11287004-Animals,
pubmed-meshheading:11287004-CHO Cells,
pubmed-meshheading:11287004-Cricetinae,
pubmed-meshheading:11287004-Escherichia coli,
pubmed-meshheading:11287004-GTP-Binding Protein alpha Subunits, Gi-Go,
pubmed-meshheading:11287004-GTP-Binding Protein alpha Subunits, Gq-G11,
pubmed-meshheading:11287004-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:11287004-Heterotrimeric GTP-Binding Proteins,
pubmed-meshheading:11287004-Protein Binding,
pubmed-meshheading:11287004-Protein Subunits,
pubmed-meshheading:11287004-Rats,
pubmed-meshheading:11287004-Receptors, Neurotensin,
pubmed-meshheading:11287004-Recombinant Fusion Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Functional coupling with Galpha(q) and Galpha(i1) protein subunits promotes high-affinity agonist binding to the neurotensin receptor NTS-1 expressed in Escherichia coli.
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pubmed:affiliation |
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. rkg@mrc-lmb.cam.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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