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J. Biol. Chem., Vol. 280, Issue 52, 42573-42579, December 30, 2005

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Transmembrane Domain-induced Oligomerization Is Crucial for the Functions of Syndecan-2 and Syndecan-4^*

Sungmun Choi1, Eunjung Lee1, Soojin Kwon, Haein Park, Jae Youn Yi, Seungin Kim, Inn-Oc Han, Yungdae Yun, and Eok-Soo Oh2

From the Department of Life Sciences, Division of Molecular Life Sciences and Center for Cell Signaling Research, Ewha Womans University, Seoul 120-750, Korea and the College of Medicine, Department of Physiology and Biophysics, Inha University, Incheon 402-751, Korea

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 C activation or in syndecan-2mediated 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.

Received for publication, August 22, 2005

^* This work was supported in part by Korea Research Foundation Grant KRF-99-042-D00096, KRF-2002-CP0327 (to E.-S. O) and in part by Korea Science and Engineering Foundation (KOSEF) through the Center for Cell Signaling Research at Ewha Womans University. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this study and were supported by a fellowship from the Brain Korea 21 project.

² To whom correspondence should be addressed: Center for Cell Signaling Research, Ewha Womans University, Daehyun-dong, Seodaemoon-Gu, Seoul 120-750 Korea. Tel.: 82-2-3277-3761; Fax: 82-2-3277-3760; E-mail: OhES{at}ewha.ac.kr.

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