| pubmed-article:18952127 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18952127 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:18952127 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:18952127 | lifeskim:mentions | umls-concept:C0205107 | lld:lifeskim |
| pubmed-article:18952127 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:18952127 | lifeskim:mentions | umls-concept:C0118022 | lld:lifeskim |
| pubmed-article:18952127 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:18952127 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:18952127 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:18952127 | pubmed:dateCreated | 2009-1-26 | lld:pubmed |
| pubmed-article:18952127 | pubmed:abstractText | Formyl peptide receptor (FPR) is a chemoattractant G protein-coupled receptor (GPCR) involved in the innate immune response against bacteria. Receptor activation is terminated by receptor phosphorylation of two serine- and threonine-rich regions located in the distal half of the cytoplasmic tail. In this study we show that introduction of an amino acid with a bulky side chain (leucine or glutamine) adjacent to a single leucine, L320, in the membrane-proximal half of the cytoplasmic tail, significantly enhanced receptor phosphorylation, beta-arrestin1/2 translocation, and receptor endocytosis, without affecting G(i)-mediated ERK1/2 activation and release of intracellular calcium. In addition, the point mutations resulted in diminished susceptibility to trypsin, suggesting a conformation different from that of wild type FPR. Alignment of the FPR sequence with the rhodopsin sequence showed that L320 resides immediately C-terminal of an amphipathic region that in rhodopsin forms helix 8. Deletion of seven amino acids (Delta309-315) from the predicted helix 8 of FPR (G307-S319) caused reduced cell signaling as well as defects in receptor phosphorylation, beta-arrestin1/2 translocation and endocytosis. Thus, the amino acid content in the N-terminal half of the cytoplasmic tail influences the structure and desensitization of FPR. | lld:pubmed |
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| pubmed-article:18952127 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18952127 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18952127 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18952127 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18952127 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18952127 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18952127 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:18952127 | pubmed:author | pubmed-author:JesaitisAlgir... | lld:pubmed |
| pubmed-article:18952127 | pubmed:author | pubmed-author:SuvorovaElena... | lld:pubmed |
| pubmed-article:18952127 | pubmed:author | pubmed-author:MiettinenHein... | lld:pubmed |
| pubmed-article:18952127 | pubmed:author | pubmed-author:GripentrogJea... | lld:pubmed |
| pubmed-article:18952127 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18952127 | pubmed:volume | 1793 | lld:pubmed |
| pubmed-article:18952127 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18952127 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18952127 | pubmed:pagination | 406-17 | lld:pubmed |
| pubmed-article:18952127 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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| pubmed-article:18952127 | pubmed:meshHeading | pubmed-meshheading:18952127... | lld:pubmed |
| pubmed-article:18952127 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:18952127 | pubmed:articleTitle | Agonist-dependent phosphorylation of the formyl peptide receptor is regulated by the membrane proximal region of the cytoplasmic tail. | lld:pubmed |
| pubmed-article:18952127 | pubmed:affiliation | Department of Microbiology, Montana State University, 109 Lewis Hall, Bozeman, MT 59717, USA. | lld:pubmed |
| pubmed-article:18952127 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18952127 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18952127 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:2357 | entrezgene:pubmed | pubmed-article:18952127 | lld:entrezgene |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18952127 | lld:pubmed |
