Agonist-induced trafficking of the low-affinity formyl peptide receptor FPRL1 Export

@article{citeulike:2870425, abstract = {The formyl peptide-like receptor FPRL1 is a member of the chemoattractant subfamily of G protein- coupled receptors involved in regulating leukocyte migration in inflammation. To elucidate mechanisms underlying the internalization of ligand-bound FPRL1 and possible receptor recycling, we characterized the endocytic itinerary of FPRL1. We show that agonist-triggered internalization from the plasma membrane into intracellular compartments is prevented by perturbation of clathrin-mediated endocytosis, such as expression of the dominant-negative clathrin Hub mutant, siRNA-mediated depletion of cellular clathrin and expression of a dominant-negative mutant of the large GTPase dynamin. Internalized FPRL1 co-localized with endocytosed transferrin and the small GTPases Rab4 and Rab11 in vesicular structures most resembling recycling endosomes. Recycling of FPRL1 was significantly reduced by pretreatment with PI3-kinase inhibitors. Thus, ligand-bound FPRL1 undergoes primarily clathrin-mediated and dynamin-dependent endocytosis and the receptor recycles via a rapid PI3-kinase-sensitive route as well as pathways involving perinuclear recycling endosomes.}, author = {Ernst, S. and Zobiack, N. and Boecker, K. and Gerke, V. and Rescher, U.}, citeulike-article-id = {2870425}, citeulike-linkout-0 = {http://dx.doi.org/10.1007/s00018-004-4116-x}, day = {1}, doi = {10.1007/s00018-004-4116-x}, journal = {Cellular and Molecular Life Sciences (CMLS)}, keywords = {fpr}, month = {June}, number = {13}, pages = {1684--1692}, posted-at = {2008-06-06 21:53:27}, priority = {2}, title = {Agonist-induced trafficking of the low-affinity formyl peptide receptor FPRL1}, url = {http://dx.doi.org/10.1007/s00018-004-4116-x}, volume = {61}, year = {2004} }

TY - JOUR ID - citeulike:2870425 L3 - citeulike-article-id:2870425 N2 - The formyl peptide-like receptor FPRL1 is a member of the chemoattractant subfamily of G protein- coupled receptors involved in regulating leukocyte migration in inflammation. To elucidate mechanisms underlying the internalization of ligand-bound FPRL1 and possible receptor recycling, we characterized the endocytic itinerary of FPRL1. We show that agonist-triggered internalization from the plasma membrane into intracellular compartments is prevented by perturbation of clathrin-mediated endocytosis, such as expression of the dominant-negative clathrin Hub mutant, siRNA-mediated depletion of cellular clathrin and expression of a dominant-negative mutant of the large GTPase dynamin. Internalized FPRL1 co-localized with endocytosed transferrin and the small GTPases Rab4 and Rab11 in vesicular structures most resembling recycling endosomes. Recycling of FPRL1 was significantly reduced by pretreatment with PI3-kinase inhibitors. Thus, ligand-bound FPRL1 undergoes primarily clathrin-mediated and dynamin-dependent endocytosis and the receptor recycles via a rapid PI3-kinase-sensitive route as well as pathways involving perinuclear recycling endosomes. IS - 13 JF - Cellular and Molecular Life Sciences (CMLS) EP - 1692 TI - Agonist-induced trafficking of the low-affinity formyl peptide receptor FPRL1 VL - 61 SP - 1684 KW - fpr AU - Ernst, S AU - Zobiack, N AU - Boecker, K AU - Gerke, V AU - Rescher, U PY - 2004/06/01/ UR - http://dx.doi.org/10.1007/s00018-004-4116-x ER -