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The oligomeric status of syndecan-4 regulates syndecan-4 interaction with alpha-actinin

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  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    4th 2009 Annual Meeting of Korean Society for Glycoscience in 2009 (2009.11)바로가기
  • 페이지
    pp.37-37
  • 저자
    Youngsil Choi, Seungin Kim, Junghyun Lee, Sung-gun Ko, Weontae Lee, Inn-Oc Han, Anne Woods, Eok-Soo Oh
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A192513

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원문정보

초록

영어
Syndecan-4, a cell surface heparan sulfate proteoglycan, is known to regulate the organization of the cytoskeleton and oligomerization is crucial for syndecan-4 function. We therefore explored a possible regulatory role of syndecan-4 oligomerization on the syndecan-4 link to cytoskeleton. Glutathione-S-transferase-syndecan-4 proteins were used to show that syndecan-4 interacted specifically with a-actinin, but not paxillin, talin, and vinculin. Interestingly, only dimeric, and not monomeric, recombinant syndecan-4 interacted with a-actinin in the presence of phosphatidylinositol 4,5-bisphosphate (PIP2), and PIP2 potentiated the interaction of both the cytopasmic domain syndecan-4 peptide and recombinant syndecan-4 proteins with a-actinin, implying that oligomerization of syndecan-4 was importance for this interaction. Consistent with this notion, a-actinin interaction was largely absent in syndecan-4 mutants defective in transmembrane domain-induced oligomerization and a-actinin-associated focal adhesions were decreased in REFs expressing syndecan-4 mutant, compared to that of wild type syndecan-4. Besides, this interaction was consistently lower with the phosphorylation-mimicking syndecan-4 mutant S183E which is known to destabilize the oligomerization of syndecan-4 cytoplasmic domain. Taken together, the data suggest that the oligomeric status of the syndecan-4 plays a crucial role in regulating the interaction of syndecan-4 with a-actinin.

저자

  • Youngsil Choi [ Department of Life Sciences, Division of Life and Pharmaceutical Sciences and the Center for Cell Signaling & Drug Discovery Research, Ewha Womans University, Seoul ]
  • Seungin Kim [ Department of Life Sciences, Division of Life and Pharmaceutical Sciences and the Center for Cell Signaling & Drug Discovery Research, Ewha Womans University, Seoul ]
  • Junghyun Lee [ Department of Life Sciences, Division of Life and Pharmaceutical Sciences and the Center for Cell Signaling & Drug Discovery Research, Ewha Womans University, Seoul ]
  • Sung-gun Ko [ Department of Biochemistry and Protein Network Research Center, College of Science, Yonsei University, Seoul 120-749 Korea ]
  • Weontae Lee [ Department of Biochemistry and Protein Network Research Center, College of Science, Yonsei University, Seoul 120-749 Korea ]
  • Inn-Oc Han [ Department of Physiology and Biophysics, Inha University, Incheon 402-751, Korea ]
  • Anne Woods [ Department of Cell Biology, University of Alabama at Birmingham 36524, USA ]
  • Eok-Soo Oh [ Department of Life Sciences, Division of Life and Pharmaceutical Sciences and the Center for Cell Signaling & Drug Discovery Research, Ewha Womans University, Seoul ]

참고문헌

자료제공 : 네이버학술정보

간행물 정보

발행기관

  • 발행기관명
    한국당과학회 [Korean Society for Glycoscience]
  • 설립연도
    2006
  • 분야
    의약학>약학
  • 소개
    본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.

간행물

  • 간행물명
    한국당과학회 학술대회
  • 간기
    연간
  • 수록기간
    2006~2022
  • 십진분류
    KDC 517 DDC 614

이 권호 내 다른 논문 / 한국당과학회 학술대회 4th 2009 Annual Meeting of Korean Society for Glycoscience in 2009

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