UM
Phosphorylation of the N-formyl peptide receptor is required for receptor internalization but not chemotaxis
Hsu M.H.; Chiang S.C.; Ye R.D.; Prossnitz E.R.
1997-11-21
Source PublicationJournal of Biological Chemistry
ISSN00219258
Volume272Issue:47Pages:29426-29429
AbstractThe human N-formyl peptide receptor (FPR) is a member of the family of leukocyte, G protein-coupled, chemoattractant receptors. To determine the role(s) of receptor phosphorylation in FPR processing and formylmethionylleucylphenylalanine (fMLF)-mediated chemotaxis, we utilized U937 cells expressing the recombinant wild type receptor and a mutant form of the FPR. This mutant, which lacks all of the serine and threonine residues in the C terminus of the receptor, ΔST, has recently been shown to produce a receptor capable of fMLF binding and G protein activation but was demonstrated not to undergo fMLF-dependent phosphorylation or desensitization of the calcium mobilization response upon repeated exposure to agonist (Prossnitz, E. R. (1997) J. Biol. Chem. 272, 15213-15219). In this report, we examined the role of receptor phosphorylation in FPR internalization and leukocyte chemotaxis. Whereas the wild type receptor was rapidly internalized upon stimulation, the phosphorylation-deficient mutant was not, remaining entirely on the cell surface. In addition, contrary to the hypothesis that receptor processing and recycling are required for chemotaxis, we found no defect in the ability of the mutant FPR to migrate up a concentration gradient of fMLF. These results indicate that phosphorylation of the FPR is a necessary step in receptor internalization but that receptor phosphorylation, desensitization, and internalization are not required for chemotaxis.
DOI10.1074/jbc.272.47.29426
URLView the original
Language英語
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Cited Times [WOS]:60   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionUniversity of Macau
AffiliationScripps Research Institute
Recommended Citation
GB/T 7714
Hsu M.H.,Chiang S.C.,Ye R.D.,et al. Phosphorylation of the N-formyl peptide receptor is required for receptor internalization but not chemotaxis[J]. Journal of Biological Chemistry,1997,272(47):29426-29429.
APA Hsu M.H.,Chiang S.C.,Ye R.D.,&Prossnitz E.R..(1997).Phosphorylation of the N-formyl peptide receptor is required for receptor internalization but not chemotaxis.Journal of Biological Chemistry,272(47),29426-29429.
MLA Hsu M.H.,et al."Phosphorylation of the N-formyl peptide receptor is required for receptor internalization but not chemotaxis".Journal of Biological Chemistry 272.47(1997):29426-29429.
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