{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vistein R"],"funding":["NIDA NIH HHS"],"pagination":["15289-94"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3780909"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["110(38)"],"pubmed_abstract":["The postendocytic recycling of signaling receptors is subject to multiple requirements. Why this is so, considering that many other proteins can recycle without apparent requirements, is a fundamental question. Here we show that cells can leverage these requirements to switch the recycling of the beta-2 adrenergic receptor (B2AR), a prototypic signaling receptor, between sequence-dependent and bulk recycling pathways, based on extracellular signals. This switch is determined by protein kinase A-mediated phosphorylation of B2AR on the cytoplasmic tail. The phosphorylation state of B2AR dictates its partitioning into spatially and functionally distinct endosomal microdomains mediating bulk and sequence-dependent recycling, and also regulates the rate of B2AR recycling and resensitization. Our results demonstrate that G protein-coupled receptor recycling is not always restricted to the sequence-dependent pathway, but may be reprogrammed as needed by physiological signals. Such flexible reprogramming might provide a versatile method for rapidly modulating cellular responses to extracellular signaling."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Reprogramming of G protein-coupled receptor recycling and signaling by a kinase switch."],"pmcid":["PMC3780909"],"funding_grant_id":["R00-DA024698","T90-DA023420","R00 DA024698","R90 DA023420"],"pubmed_authors":["Vistein R","Puthenveedu MA"],"additional_accession":[]},"is_claimable":false,"name":"Reprogramming of G protein-coupled receptor recycling and signaling by a kinase switch.","description":"The postendocytic recycling of signaling receptors is subject to multiple requirements. Why this is so, considering that many other proteins can recycle without apparent requirements, is a fundamental question. Here we show that cells can leverage these requirements to switch the recycling of the beta-2 adrenergic receptor (B2AR), a prototypic signaling receptor, between sequence-dependent and bulk recycling pathways, based on extracellular signals. This switch is determined by protein kinase A-mediated phosphorylation of B2AR on the cytoplasmic tail. The phosphorylation state of B2AR dictates its partitioning into spatially and functionally distinct endosomal microdomains mediating bulk and sequence-dependent recycling, and also regulates the rate of B2AR recycling and resensitization. Our results demonstrate that G protein-coupled receptor recycling is not always restricted to the sequence-dependent pathway, but may be reprogrammed as needed by physiological signals. Such flexible reprogramming might provide a versatile method for rapidly modulating cellular responses to extracellular signaling.","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Sep","modification":"2025-04-20T03:19:07.96Z","creation":"2019-03-27T01:16:27Z"},"accession":"S-EPMC3780909","cross_references":{"pubmed":["24003153"],"doi":["10.1073/pnas.1306340110"]}}