Transmembrane domain-induced oligomerization is crucial for the functions of syndecan-2 and syndecan-4

Sungmun Choi, Eunjung Lee, Soojin Kwon, Haein Park, Jae Youn Yi, Seungin Kim, Inn Oc Han, Yungdae Yun, Eok Soo Oh

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92 Scopus citations


The syndecans are known to form homologous oligomers that may be important for their functions. We have therefore determined the role of oligomerization of syndecan-2 and syndecan-4. A series of glutathione S-transferase-syndecan-2 and syndecan-4 chimeric proteins showed that all syndecan constructs containing the transmembrane domain formed SDS-resistant dimers, but not those lacking it. SDS-resistant dimer formation was hardly seen in the syndecan chimeras where each transmembrane domain was substituted with that of platelet-derived growth factor receptor (PDGFR). Increased MAPK activity was detected in HEK293T cells transfected with syndecan/PDGFR chimeras in a syndecan transmembrane domain-dependent fashion. The chimera-induced MAPK activation was independent of both ligand and extracellular domain, implying that the transmembrane domain is sufficient to induce dimerization/oligomerization in vivo. Furthermore, the syndecan chimeras were defective in syndecan-4-mediated focal adhesion formation and protein kinase Cα activation or in syndecan-2-mediated cell migration. Taken together, these data suggest that the transmembrane domains are sufficient for inducing dimerization and that transmembrane domain-induced oligomerization is crucial for syndecan-2 and syndecan-4 functions.

Original languageEnglish
Pages (from-to)42573-42579
Number of pages7
JournalJournal of Biological Chemistry
Issue number52
StatePublished - 30 Dec 2005


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