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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 M.-J.Park J.Jang S.Eom C.-Y.Oh E.-S.
Ewha Authors
오억수
SCOPUS Author ID
오억수scopus
Issue Date
2016
Journal Title
Journal of Biological Chemistry
ISSN
0021-9258JCR Link
Citation
vol. 291, no. 2, pp. 872 - 881
Publisher
American Society for Biochemistry and Molecular Biology Inc.
Indexed
SCI; SCIE; SCOPUS scopus
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 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. © 2016 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A.
DOI
10.1074/jbc.M115.685040
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자연과학대학 > 생명과학전공 > Journal papers
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