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Abstracts for poster Presentation

Unique high-order oligomerization of syndecan-3 is induced by the transmembrane domain

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초록

영어

Syndecans are a cell surface single-pass transmembrane protein which is involved in various cellular functions. It is known that syndecans form homo-, hetero-dimer through transmembrane domain and the extent of dimerization affects intracellular signaling. However, little has been known about transmembrane domain of syndecan-3. In this research, it is discovered that syndecan-3 forms SDS-resistant higher-order oligomerization through transmembrane domain and alanine located nearby GxxxG motif has a crucial role to maintain oligomer among 25 hydrophobic transmembrane amino acids. Moreover, the pattern of higher-order oligomerization has an influence to regulate cellular function such as migration in neuroblastoma. In conclusion, syndecan-3 has a distinct feature of higher-order oligomerization through transmembrane domain in constrast with other syndecan family proteins and alanine is a key amino acid which has an ability to form oligomer and also these pattern of oligomerization in syndecan-3 is linked to cell behavior.

저자정보

  • Min Ji Han Department of Life Sciences, Ewha Womans University
  • Eok-Soo Oh Department of Life Sciences, Ewha Womans University

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