Source:http://linkedlifedata.com/resource/pubmed/id/11351280
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
2001-5-14
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| pubmed:abstractText |
To analyse the mechanisms of PAR-1 internalisation, we constructed several PAR-1 mutants and stably expressed them in CHO cells. Our study shows that the Ser(306)-->Ala mutation (S306A), which eliminates a potential site of phosphorylation by PKC in the third intracellular loop of PAR-1, did not change the rate of phosphorylation but reduced the rate of thrombin-induced internalisation of the PAR-1 mutant (58 versus 78% of membrane PAR-1 in 15 min, p<0.005). Deletion of the last 43 amino acid residues of the PAR-1 cytoplasmic tail completely suppressed the thrombin phosphorylation of the mutated receptor and significantly reduced its internalisation upon activation. This deletion also inhibited the PMA-induced and the agonist-independent internalisation of the receptor. The Tyr(371)--> Ala mutation (Y371A), in a NPXXY motif of the seventh transmembrane domain of the receptor had no effect on the receptor behaviour. Our results indicate that both the C-tail and the third intracellular loop are involved in PAR-1 internalisation induced by thrombin while only the C-tail plays a role in the PMA-induced and in the agonist-independent PAR-1 internalisation.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, PAR-1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thrombin,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
1107-3756
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
7
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
653-8
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11351280-Alanine,
pubmed-meshheading:11351280-Animals,
pubmed-meshheading:11351280-Binding Sites,
pubmed-meshheading:11351280-CHO Cells,
pubmed-meshheading:11351280-Cricetinae,
pubmed-meshheading:11351280-Cytoplasm,
pubmed-meshheading:11351280-Gene Deletion,
pubmed-meshheading:11351280-Mutation,
pubmed-meshheading:11351280-Phosphorylation,
pubmed-meshheading:11351280-Plasmids,
pubmed-meshheading:11351280-Precipitin Tests,
pubmed-meshheading:11351280-Protein Kinase C,
pubmed-meshheading:11351280-Protein Structure, Tertiary,
pubmed-meshheading:11351280-Receptor, PAR-1,
pubmed-meshheading:11351280-Receptors, Thrombin,
pubmed-meshheading:11351280-Thrombin,
pubmed-meshheading:11351280-Time Factors,
pubmed-meshheading:11351280-Transfection,
pubmed-meshheading:11351280-Tyrosine
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| pubmed:year |
2001
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| pubmed:articleTitle |
Internalisation of the protease-activated receptor 1: role of the third intracellular loop and of the cytoplasmic tail.
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| pubmed:affiliation |
INSERM U489, Association Claude Bernard, Hôpital Tenon, 75970 Paris cedex 20, France.
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| pubmed:publicationType |
Journal Article
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