Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 오억수 | - |
dc.date.accessioned | 2016-12-27T02:12:24Z | - |
dc.date.available | 2016-12-27T02:12:24Z | - |
dc.date.issued | 2016 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.other | OAK-19744 | - |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/233151 | - |
dc.description.abstract | The PDZ domain-containing scaffold protein, syntenin-1, binds to the transmembrane proteoglycan, syndecan-4, but the molecular mechanism/function of this interaction are unknown. Crystal structure analysis of syntenin-1/syndecan-4 cytoplasmic domains revealed that syntenin-1 forms a symmetrical pair of dimers anchored by a syndecan-4 dimer. The syndecan-4 cytoplasmic domain is a compact intertwined dimer with a symmetrical clamp shape and two antiparallel strands forming a cavity within the dimeric twist. The PDZ2 domain of syntenin-1 forms a direct antiparallel interaction with the syndecan-4 cytoplasmic domain, inhibiting the functions of syndecan-4 such as focal adhesion formation. Moreover, C-terminal region of syntenin-1 reveals an essential role for enhancing the molecular homodimerization. Mutation of key syntenin-1 residues involved in the syndecan-4 interaction or homodimer formation abolishes the inhibitory function of syntenin-1, as does deletion of the homodimerization-related syntenin-1 C-terminal domain. Syntenin-1, but not dimer-formation-incompetent mutants, rescued the syndecan-4-mediated inhibition of migration and pulmonary metastasis by B16F10 cells. Therefore, we conclude that syntenin-1 negatively regulates syndecan-4 function via oligomerization and/or syndecan-4 interaction, impacting cytoskeletal organization and cell migration. © The Author(s) 2016. | - |
dc.language | English | - |
dc.publisher | Nature Publishing Group | - |
dc.title | New structural insight of C-terminal region of Syntenin-1, enhancing the molecular dimerization and inhibitory function related on Syndecan-4 signaling | - |
dc.type | Article | - |
dc.relation.volume | 6 | - |
dc.relation.index | SCIE | - |
dc.relation.index | SCOPUS | - |
dc.relation.journaltitle | Scientific Reports | - |
dc.identifier.doi | 10.1038/srep36818 | - |
dc.identifier.wosid | WOS:000387872800001 | - |
dc.identifier.scopusid | 2-s2.0-84994868782 | - |
dc.author.google | Choi Y. | - |
dc.author.google | Yun J.-H. | - |
dc.author.google | Yoo J. | - |
dc.author.google | Lee I. | - |
dc.author.google | Kim H. | - |
dc.author.google | Son H.-N. | - |
dc.author.google | Kim I.-S. | - |
dc.author.google | Yoon H.S. | - |
dc.author.google | Zimmermann P. | - |
dc.author.google | Couchman J.R. | - |
dc.author.google | Cho H.-S. | - |
dc.author.google | Oh E.-S. | - |
dc.author.google | Lee W. | - |
dc.contributor.scopusid | 오억수(7101967153) | - |
dc.date.modifydate | 20230201093717 | - |