| http://purl.uniprot.org/citations/18641122 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18641122 | http://www.w3.org/2000/01/rdf-schema#comment | "Phosphorylation of the polarity protein Par-3 by the serine/threonine kinases aPKCzeta/iota and Par-1 (EMK1/MARK2) regulates various aspects of epithelial cell polarity, but little is known about the mechanisms by which these posttranslational modifications are reversed. We find that the serine/threonine protein phosphatase PP1 (predominantly the alpha isoform) binds Par-3, which localizes to tight junctions in MDCKII cells. PP1alpha can associate with multiple sites on Par-3 while retaining its phosphatase activity. By using a quantitative mass spectrometry-based technique, multiple reaction monitoring, we show that PP1alpha specifically dephosphorylates Ser-144 and Ser-824 of mouse Par-3, as well as a peptide encompassing Ser-885. Consistent with these observations, PP1alpha regulates the binding of 14-3-3 proteins and the atypical protein kinase C (aPKC) zeta to Par-3. Furthermore, the induced expression of a catalytically inactive mutant of PP1alpha severely delays the formation of functional tight junctions in MDCKII cells. Collectively, these results show that Par-3 functions as a scaffold, coordinating both serine/threonine kinases and the PP1alpha phosphatase, thereby providing dynamic control of the phosphorylation events that regulate the Par-3/aPKC complex."xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0804102105"xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/author | "Pawson T."xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/author | "Metalnikov P."xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/author | "Traweger A."xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/author | "Taylor L."xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/author | "Wiggin G."xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/author | "Tate S.A."xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/pages | "10402-10407"xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/title | "Protein phosphatase 1 regulates the phosphorylation state of the polarity scaffold Par-3."xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://purl.uniprot.org/core/volume | "105"xsd:string |
| http://purl.uniprot.org/citations/18641122 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18641122 |
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