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http://purl.uniprot.org/citations/11684085http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11684085http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11684085http://www.w3.org/2000/01/rdf-schema#comment"Phosphoprotein associated with GEMs (PAG), also known as Csk-binding protein (Cbp), is a broadly expressed palmitoylated transmembrane adapter protein found in membrane rafts, also called GEMs (glycosphingolipid-enriched membrane microdomains). PAG is known to bind and activate the essential regulator of Src-family kinases, cytoplasmic protein tyrosine kinase Csk. In the present study we used the yeast 2-hybrid system to search for additional proteins which might bind to PAG. We have identified the abundant cytoplasmic adapter protein EBP50 (ezrin/radixin/moesin (ERM)-binding phosphoprotein of 50 kDa), also known as NHERF (Na(+)/H(+) exchanger regulatory factor), as a specific PAG-binding partner. The interaction involves the C-terminal sequence (TRL) of PAG and N-terminal PDZ domain(s) of EBP50. As EBP50 is known to interact via its C-terminal domain with the ERM-family proteins, which in turn bind to actin cytoskeleton, the PAG-EBP50 interaction may be important for connecting membrane rafts to the actin cytoskeleton."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(01)02955-6"xsd:string
http://purl.uniprot.org/citations/11684085http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(01)02955-6"xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Milgram S.L."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Milgram S.L."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Andera L."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Andera L."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Angelisova P."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Angelisova P."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Brdicka T."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Brdicka T."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Horejsi V."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Horejsi V."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Brdickova N."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Brdickova N."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Spicka J."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/author"Spicka J."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/pages"133-136"xsd:string
http://purl.uniprot.org/citations/11684085http://purl.uniprot.org/core/pages"133-136"xsd:string