Full metadata record
DC Field | Value | Language |
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dc.contributor.author | 오억수 | - |
dc.contributor.author | 장보희 | - |
dc.date.accessioned | 2020-02-07T16:30:09Z | - |
dc.date.available | 2020-02-07T16:30:09Z | - |
dc.date.issued | 2020 | - |
dc.identifier.issn | 0898-6568 | - |
dc.identifier.issn | 1873-3913 | - |
dc.identifier.other | OAK-26423 | - |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/253322 | - |
dc.description.abstract | Syndecans are single-pass transmembrane proteins on the cell surface that are involved in various cellular functions. Previously, we reported that both homo- and hetero-form of syndecan dimers affected their functionality. However, little is known about the structural role of the transmembrane domain of syndecan-3. A series of glutathione-S-transferase syndecan-3 proteins showed that syndecan-3 formed SOS-resistant dimers and oligomers. SDS-resistant oligomer formation was barely observed in the syndecan deletion mutants lacking the transmembrane domain. Interestingly, the presence of an alanine 397 residue in the transmembrane domain correlated with SDS-resistant oligomer, and its replacement by phenylalanine (AF mutant) significantly reduced SDS-resistant oligomer formation. Beside the AF mutant significantly reduced syndecan-3 mediated cellular processes such as cell adhesion, migration and neurite outgrowth of SH-SYSY neuroblastoma. Furthermore, the alanine residue regulated hetero-oligomer formation of syndecan-3, and hetero-oligomer formation significantly reduced syndecan-3-mediated neurite outgrowth of SH-SYSY cells. Taken together, all these data suggest that syndecan-3 has a specific feature of oligomerization by the transmembrane domain and this oligomerization tendency is crucial for the function of syndecan-3. | - |
dc.language | English | - |
dc.publisher | ELSEVIER SCIENCE INC | - |
dc.subject | Syndecan-3 | - |
dc.subject | Oligomerization | - |
dc.subject | Transmembrane domain | - |
dc.subject | Cell adhesion | - |
dc.title | The oligomerization mediated by the alanine 397 residue in the transmembrane domain is crucial to sydecan-3 functions | - |
dc.type | Article | - |
dc.relation.volume | 69 | - |
dc.relation.index | SCIE | - |
dc.relation.index | SCOPUS | - |
dc.relation.journaltitle | CELLULAR SIGNALLING | - |
dc.identifier.doi | 10.1016/j.cellsig.2020.109544 | - |
dc.identifier.wosid | WOS:000518868600002 | - |
dc.identifier.scopusid | 2-s2.0-85078075957 | - |
dc.author.google | Jung, Hyejung | - |
dc.author.google | Han, Minji | - |
dc.author.google | Jang, Bohee | - |
dc.author.google | Park, Eunhye | - |
dc.author.google | Oh, Eok-Soo | - |
dc.contributor.scopusid | 오억수(7101967153) | - |
dc.contributor.scopusid | 장보희(55242403100) | - |
dc.date.modifydate | 20230201093717 | - |