| http://purl.uniprot.org/citations/26601939 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26601939 | http://www.w3.org/2000/01/rdf-schema#comment | "The transmembrane domain (TMD) of the syndecans, a family of transmembrane heparin sulfate proteoglycans, is involved in forming homo- and heterodimers and oligomers that transmit signaling events. Recently, we reported that the unique phenylalanine in TMD positively regulates intramolecular interactions of syndecan-2. Besides the unique phenylalanine, syndecan-2 contains a conserved phenylalanine (SDC2-Phe-169) that is present in all syndecan TMDs, but its function has not been determined. We therefore investigated the structural role of SDC2-Phe-169 in syndecan TMDs. Replacement of SDC2-Phe-169 by tyrosine (S2F169Y) did not affect SDS-resistant homodimer formation but significantly reduced SDS-resistant heterodimer formation between syndecan-2 and -4, suggesting that SDC2-Phe-169 is involved in the heterodimerization/oligomerization of syndecans. Similarly, in an in vitro binding assay, a syndecan-2 mutant (S2(F169Y)) showed a significantly reduced interaction with syndecan-4. FRET assays showed that heteromolecular interactions between syndecan-2 and -4 were reduced in HEK293T cells transfected with S2(F169Y) compared with syndecan-2. Moreover, S2(F169Y) reduced downstream reactions mediated by the heterodimerization of syndecan-2 and -4, including Rac activity, cell migration, membrane localization of PKCα, and focal adhesion formation. The conserved phenylalanine in syndecan-1 and -3 also showed heterodimeric interaction with syndecan-2 and -4. Taken together, these findings suggest that the conserved phenylalanine in the TMD of syndecans is crucial in regulating heteromeric interactions of syndecans."xsd:string |
| http://purl.uniprot.org/citations/26601939 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m115.685040"xsd:string |
| http://purl.uniprot.org/citations/26601939 | http://purl.uniprot.org/core/author | "Park J."xsd:string |
| http://purl.uniprot.org/citations/26601939 | http://purl.uniprot.org/core/author | "Kwon M.J."xsd:string |
| http://purl.uniprot.org/citations/26601939 | http://purl.uniprot.org/core/author | "Eom C.Y."xsd:string |
| http://purl.uniprot.org/citations/26601939 | http://purl.uniprot.org/core/author | "Jang S."xsd:string |
| http://purl.uniprot.org/citations/26601939 | http://purl.uniprot.org/core/author | "Oh E.S."xsd:string |
| http://purl.uniprot.org/citations/26601939 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/26601939 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/26601939 | http://purl.uniprot.org/core/pages | "872-881"xsd:string |
| http://purl.uniprot.org/citations/26601939 | http://purl.uniprot.org/core/title | "The Conserved Phenylalanine in the Transmembrane Domain Enhances Heteromeric Interactions of Syndecans."xsd:string |
| http://purl.uniprot.org/citations/26601939 | http://purl.uniprot.org/core/volume | "291"xsd:string |
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