| http://purl.uniprot.org/citations/9660868 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9660868 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9660868 | http://www.w3.org/2000/01/rdf-schema#comment | "In Caenorhabditis elegans, mutations in the lin-2 gene inactivate the LET-23 receptor tyrosine kinase/Ras/MAP kinase pathway required for vulval cell differentiation. One function of LIN-2 is to localize LET-23 to the basal membrane domain of vulval precursor cells. LIN-2 belongs to the membrane-associated guanylate kinase family of proteins. We have cloned and characterized the human homolog of LIN-2, termed hCASK, and Northern and Western blot analyses reveal that it is ubiquitously expressed. Indirect immunofluorescence localizes CASK to distinct lateral and/or basal plasma membrane domains in different epithelial cell types. We detect in a yeast two-hybrid screen that the PDZ domain of hCASK binds to the heparan sulfate proteoglycan syndecan-2. This interaction is confirmed using in vitro binding assays and immunofluorescent colocalization. Furthermore, we demonstrate that hCASK binds the actin-binding protein 4.1. Syndecans are known to bind extracellular matrix, and to form coreceptor complexes with receptor tyrosine kinases. We speculate that CASK mediates a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with protein 4.1. Like other membrane-associated guanylate kinases, its multidomain structure enables it to act as a scaffold at the membrane, potentially recruiting multiple proteins and coordinating signal transduction."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.142.1.129"xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.142.1.129"xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Chishti A.H."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Chishti A.H."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Anderson J.M."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Anderson J.M."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Walther Z."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Walther Z."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Cohen A.R."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Cohen A.R."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Marfatia S.M."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Marfatia S.M."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Woods D.F."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/author | "Woods D.F."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/pages | "129-138"xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/pages | "129-138"xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/title | "Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells."xsd:string |
| http://purl.uniprot.org/citations/9660868 | http://purl.uniprot.org/core/title | "Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells."xsd:string |