| http://purl.uniprot.org/citations/25385611 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25385611 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25385611 | http://www.w3.org/2000/01/rdf-schema#comment | "The Crumbs (Crb) complex, formed by Crb, PALS1, and PATJ, is evolutionarily conserved in metazoans and acts as a master cell-growth and -polarity regulator at the apical membranes in polarized epithelia. Crb intracellular functions, including its direct binding to PALS1, are mediated by Crb's highly conserved 37-residue cytoplasmic tail. However, the mechanistic basis governing the highly specific Crb-PALS1 complex formation is unclear, as reported interaction between the Crb tail (Crb-CT) and PALS1 PSD-95/DLG/ZO-1 (PDZ) domain is weak and promiscuous. Here we have discovered that the PDZ-Src homolgy 3 (SH3)-Guanylate kinase (GK) tandem of PALS1 binds to Crb-CT with a dissociation constant of 70 nM, which is ∼ 100-fold stronger than the PALS1 PDZ-Crb-CT interaction. The crystal structure of the PALS1 PDZ-SH3-GK-Crb-CT complex reveals that PDZ-SH3-GK forms a structural supramodule with all three domains contributing to the tight binding to Crb. Mutations disrupting the tertiary interactions of the PDZ-SH3-GK supramodule weaken the PALS1-Crb interaction and compromise PALS1-mediated polarity establishment in Madin-Darby canine kidney (MDCK) cysts. We further show that specific target binding of other members of membrane-associated guanylate kinases (MAGUKs) (e.g., CASK binding to neurexin) also requires the presence of their PDZ-SH3-GK tandems."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1416515111"xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1416515111"xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Li Y."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Li Y."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Wei Z."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Wei Z."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Yan Y."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Yan Y."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Zhang M."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Zhang M."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Du Q."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Du Q."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Wan Q."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/author | "Wan Q."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/pages | "17444-17449"xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/pages | "17444-17449"xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/title | "Structure of Crumbs tail in complex with the PALS1 PDZ-SH3-GK tandem reveals a highly specific assembly mechanism for the apical Crumbs complex."xsd:string |
| http://purl.uniprot.org/citations/25385611 | http://purl.uniprot.org/core/title | "Structure of Crumbs tail in complex with the PALS1 PDZ-SH3-GK tandem reveals a highly specific assembly mechanism for the apical Crumbs complex."xsd:string |