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Domain structure of the plasma membrane : interaction between membrane skeleton and membrane receptors

Research Project

Project/Area Number 04833003
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field 分子細胞生物学
Research InstitutionThe University of Tokyo

Principal Investigator

SAKO Yasushi  The University of Tokyo Assist. Prof.College of Arts and Sciences, 教養学部, 助手 (20215700)

Co-Investigator(Kenkyū-buntansha) KUSUMI Akihro  The University of Tokyo Assoc.Prof.College of Arts and Sciences, 教養学部, 助教授 (50169992)
Project Period (FY) 1992 – 1993
Project Status Completed (Fiscal Year 1993)
Budget Amount *help
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1993: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1992: ¥1,400,000 (Direct Cost: ¥1,400,000)
Keywordsplasma membrane / membrane proteins / transiferrin receptor / coated pitt / adoptor complex / single particle tracking / optical twtezems / cytoskoleton / 一粒子追路法 / 膜ドメイン / 側方拡散 / 膜骨格 / レーザー光トラップ
Research Abstract

Movements of transferrin receptor molecules in the plasma membrane of cultured normal rat kidney fibroblastic cells were investigated by video-enhanced contrast optical microscopy with nanometer-level special precision and video-rate temporal resolution by lebeling the receptor with the ligand-coated 40-nm colloidal gold particles. Most of the movement trajectories are of the confined diffusion type within domains of -0.25mum^2. Movement within the domains is random with a diffusion coefficient -10^<-9> cm^2/s, which is consistent with that expected for free Brownian diffusion of proteins in the plasma membrane. The receptor molecules move from one domain to one of the adjacent domains at an average frequency of 0.034s^<-1>, indicating that the plasma membrane is compartmentalized for diffusion of membrane receptors and that long-range diffusion is the result of successive intercompartmental jumps. Partial destruction of the cytoskeleton suggest that the boundaries between compartments are made of dynamically fluctuating membrane skeletons.

Report

(3 results)
  • 1993 Annual Research Report   Final Research Report Summary
  • 1992 Annual Research Report
  • Research Products

    (6 results)

All Other

All Publications (6 results)

  • [Publications] Sako,Y.et al.: "Compartmeutalized structure of the plasmamembrane for receptor movements as revealed by a nanoweter-level motion analysis" The Jorrnal of Cell Biology. 125. 1251-1264 (1994)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] Oida, T., Sako, Y., and Kusumi, A.: "Fluorescence lifetime imaging microscopy (flimscopy). Methodology development and application to studies of endosome fusion in single cells." Biophys.J.64. 676-685 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] Kusumi, A., Sako, Y., and Yamamoto, M.: "Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells." Biophys.J.65. 2021-2040 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] Sako, Y.and Kusumi, A.: "Compartmentalized structure of the plasma membrane for receptor movements as revealed by a nanometer-level motion analysis." J.Cell Biol.125. 1251-1264 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] Kusumi A.et al.: "Confined lateral diffusion of membrane receptors as observed by single particle tracking(nanovid microscopy):Effects of calcium-induced differentiation of epithelial cells." Biophysical Journal. 65. 2021-2040 (1993)

    • Related Report
      1993 Annual Research Report
  • [Publications] Oida,T.et al.: "Fluorescence lifotime imaging microscopy(flimscopy).Methodology development and application to studies of endosome fusion in single cells." Biophysical Journal. (1993)

    • Related Report
      1992 Annual Research Report

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Published: 1992-04-01   Modified: 2016-04-21  

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