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The Conserved Phenylalanine in the Transmembrane Domain Enhances Heteromeric Interactions of Syndecans
- Title
- The Conserved Phenylalanine in the Transmembrane Domain Enhances Heteromeric Interactions of Syndecans
- Authors
- Kwon, Mi-Jung; Park, Jisu; Jang, Sinae; Eom, Chi-Yong; Oh, Eok-Soo
- Ewha Authors
- 오억수
- SCOPUS Author ID
- 오억수
- Issue Date
- 2016
- Journal Title
- JOURNAL OF BIOLOGICAL CHEMISTRY
- ISSN
- 1083-351X
- Citation
- JOURNAL OF BIOLOGICAL CHEMISTRY vol. 291, no. 2, pp. 872 - 881
- Publisher
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- Indexed
- SCIE; SCOPUS
- Document Type
- Article
- Abstract
- 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 PKC alpha, 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.
- DOI
- 10.1074/jbc.M115.685040
- Appears in Collections:
- 자연과학대학 > 생명과학전공 > Journal papers
- Files in This Item:
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