View : 626 Download: 0
The oligomerization mediated by the alanine 397 residue in the transmembrane domain is crucial to sydecan-3 functions
- Title
- The oligomerization mediated by the alanine 397 residue in the transmembrane domain is crucial to sydecan-3 functions
- Authors
- Jung, Hyejung; Han, Minji; Jang, Bohee; Park, Eunhye; Oh, Eok-Soo
- Ewha Authors
- 오억수; 장보희
- SCOPUS Author ID
- 오억수; 장보희
- Issue Date
- 2020
- Journal Title
- CELLULAR SIGNALLING
- ISSN
- 0898-6568
1873-3913
- Citation
- CELLULAR SIGNALLING vol. 69
- Keywords
- Syndecan-3; Oligomerization; Transmembrane domain; Cell adhesion
- Publisher
- ELSEVIER SCIENCE INC
- Indexed
- SCIE; SCOPUS
- Document Type
- Article
- 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.
- DOI
- 10.1016/j.cellsig.2020.109544
- Appears in Collections:
- 자연과학대학 > 생명과학전공 > Journal papers
- Files in This Item:
There are no files associated with this item.
- Export
- RIS (EndNote)
- XLS (Excel)
- XML