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• W2149420045 abstract "Postendocytic sorting of G protein-coupled receptors (GPCRs) is driven by their interactions between highly diverse receptor sequence motifs with their interacting proteins, such as postsynaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), zonula occludens-1 protein (zo-1) (PDZ) domain proteins. However, whether these diverse interactions provide an underlying functional specificity, in addition to driving sorting, is unknown. Here we identify GPCRs that recycle via distinct PDZ ligand/PDZ protein pairs that exploit their recycling machinery primarily for targeted endosomal localization and signaling specificity. The luteinizing hormone receptor (LHR) and β2-adrenergic receptor (B2AR), two GPCRs sorted to the regulated recycling pathway, underwent divergent trafficking to distinct endosomal compartments. Unlike B2AR, which traffics to early endosomes (EE), LHR internalizes to distinct pre-early endosomes (pre-EEs) for its recycling. Pre-EE localization required interactions of the LHR C-terminal tail with the PDZ protein GAIP-interacting protein C terminus, inhibiting its traffic to EEs. Rerouting the LHR to EEs, or EE-localized GPCRs to pre-EEs, spatially reprograms MAPK signaling. Furthermore, LHR-mediated activation of MAPK signaling requires internalization and is maintained upon loss of the EE compartment. We propose that combinatorial specificity between GPCR sorting sequences and interacting proteins dictates an unprecedented spatiotemporal control in GPCR signal activity. Postendocytic sorting of G protein-coupled receptors (GPCRs) is driven by their interactions between highly diverse receptor sequence motifs with their interacting proteins, such as postsynaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), zonula occludens-1 protein (zo-1) (PDZ) domain proteins. However, whether these diverse interactions provide an underlying functional specificity, in addition to driving sorting, is unknown. Here we identify GPCRs that recycle via distinct PDZ ligand/PDZ protein pairs that exploit their recycling machinery primarily for targeted endosomal localization and signaling specificity. The luteinizing hormone receptor (LHR) and β2-adrenergic receptor (B2AR), two GPCRs sorted to the regulated recycling pathway, underwent divergent trafficking to distinct endosomal compartments. Unlike B2AR, which traffics to early endosomes (EE), LHR internalizes to distinct pre-early endosomes (pre-EEs) for its recycling. Pre-EE localization required interactions of the LHR C-terminal tail with the PDZ protein GAIP-interacting protein C terminus, inhibiting its traffic to EEs. Rerouting the LHR to EEs, or EE-localized GPCRs to pre-EEs, spatially reprograms MAPK signaling. Furthermore, LHR-mediated activation of MAPK signaling requires internalization and is maintained upon loss of the EE compartment. We propose that combinatorial specificity between GPCR sorting sequences and interacting proteins dictates an unprecedented spatiotemporal control in GPCR signal activity." @default.
• W2149420045 created "2016-06-24" @default.
• W2149420045 creator A5007160724 @default.
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• W2149420045 creator A5057829483 @default.
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• W2149420045 date "2014-02-01" @default.
• W2149420045 modified "2023-10-17" @default.
• W2149420045 title "Spatially Restricted G Protein-coupled Receptor Activity via Divergent Endocytic Compartments" @default.
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• W2149420045 cites W1595083713 @default.
• W2149420045 cites W1751435293 @default.
• W2149420045 cites W1889864283 @default.
• W2149420045 cites W1966311581 @default.
• W2149420045 cites W1967182910 @default.
• W2149420045 cites W1968578345 @default.
• W2149420045 cites W1969464978 @default.
• W2149420045 cites W1975510716 @default.
• W2149420045 cites W1987038656 @default.
• W2149420045 cites W1998079639 @default.
• W2149420045 cites W2000412654 @default.
• W2149420045 cites W2000531537 @default.
• W2149420045 cites W2017886031 @default.
• W2149420045 cites W2019245431 @default.
• W2149420045 cites W2022586583 @default.
• W2149420045 cites W2025973335 @default.
• W2149420045 cites W2027076158 @default.
• W2149420045 cites W2027639590 @default.
• W2149420045 cites W2041097342 @default.
• W2149420045 cites W2041715648 @default.
• W2149420045 cites W2042041059 @default.
• W2149420045 cites W2042698502 @default.
• W2149420045 cites W2049253479 @default.
• W2149420045 cites W2052640354 @default.
• W2149420045 cites W2054883747 @default.
• W2149420045 cites W2061098391 @default.
• W2149420045 cites W2066964651 @default.
• W2149420045 cites W2067166210 @default.
• W2149420045 cites W2069006856 @default.
• W2149420045 cites W2069083396 @default.
• W2149420045 cites W2069981183 @default.
• W2149420045 cites W2073456836 @default.
• W2149420045 cites W2074325696 @default.
• W2149420045 cites W2077591028 @default.
• W2149420045 cites W2082215793 @default.
• W2149420045 cites W2082379606 @default.
• W2149420045 cites W2082817154 @default.
• W2149420045 cites W2085004994 @default.
• W2149420045 cites W2090664128 @default.
• W2149420045 cites W2091659381 @default.
• W2149420045 cites W2091884933 @default.
• W2149420045 cites W2094788934 @default.
• W2149420045 cites W2095250075 @default.
• W2149420045 cites W2101849511 @default.
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• W2149420045 cites W2108187046 @default.
• W2149420045 cites W2116354283 @default.
• W2149420045 cites W2117754393 @default.
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• W2149420045 cites W2137850079 @default.
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• W2149420045 doi "https://doi.org/10.1074/jbc.m113.526350" @default.
• W2149420045 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3924264" @default.
• W2149420045 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24375413" @default.
• W2149420045 hasPublicationYear "2014" @default.
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