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http://purl.uniprot.org/citations/12604586http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12604586http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12604586http://www.w3.org/2000/01/rdf-schema#comment"The adaptor protein complex-1 (AP-1) sorts and packages membrane proteins into clathrin-coated vesicles (CCVs) at the TGN and endosomes. Here we show that this process is highly regulated by phosphorylation of AP-1 subunits. Cell fractionation studies revealed that membrane-associated AP-1 differs from cytosolic AP-1 in the phosphorylation status of its beta1 and mu1 subunits. AP-1 recruitment onto the membrane is associated with protein phosphatase 2A (PP2A)-mediated dephosphorylation of its beta1 subunit, which enables clathrin assembly. This Golgi-associated isoform of PP2A exhibits specificity for phosphorylated beta1 compared with phosphorylated mu1. Once on the membrane, the mu1 subunit undergoes phosphorylation, which results in a conformation change, as revealed by increased sensitivity to trypsin. This conformational change is associated with increased binding to sorting signals on the cytoplasmic tails of cargo molecules. Dephosphorylation of mu1 (and mu2) by another PP2A-like phosphatase reversed the effect and resulted in adaptor release from CCVs. Immunodepletion and okadaic acid inhibition studies demonstrate that PP2A is the cytosolic cofactor for Hsc-70-mediated adaptor uncoating. A model is proposed where cyclical phosphorylation/dephosphorylation of the subunits of AP-1 regulate its function from membrane recruitment until its release into cytosol."xsd:string
http://purl.uniprot.org/citations/12604586http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200211080"xsd:string
http://purl.uniprot.org/citations/12604586http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200211080"xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/author"Ghosh P."xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/author"Ghosh P."xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/author"Kornfeld S."xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/author"Kornfeld S."xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/pages"699-708"xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/pages"699-708"xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/title"AP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylation."xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/title"AP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylation."xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/volume"160"xsd:string
http://purl.uniprot.org/citations/12604586http://purl.uniprot.org/core/volume"160"xsd:string
http://purl.uniprot.org/citations/12604586http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12604586
http://purl.uniprot.org/citations/12604586http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12604586
http://purl.uniprot.org/citations/12604586http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12604586
http://purl.uniprot.org/citations/12604586http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12604586
http://purl.uniprot.org/uniprot/Q2KJ81http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12604586
http://purl.uniprot.org/uniprot/Q3SYW1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12604586