N-glycosylation enables high lateral mobility of GPI-anchored proteins at a molecular crowding threshold

• 田中, 求

  Department of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg･Department of Electrical Engineering, Bioelectronic Systems Lab, Columbia University

• Glogger, Marius

  Department of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg

• Jones, Nicola G.

  Department of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg

• Abuillan, Wasim

  Physical Chemistry of Biosystems, Institute of Physical Chemistry, University of Heidelberg

• Batram, Christopher

  Department of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg

• Hermann, Anne

  Department of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg

• Fenz, Susanne F.

  Department of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg

• Tanaka, Motomu

  Physical Chemistry of Biosystems, Institute of Physical Chemistry, University of Heidelberg･Institute for Integrated Cell-Material Science (WPI iCeMS), Kyoto University

• Engstler, Markus

  Department of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg

抄録

The protein density in biological membranes can be extraordinarily high, but the impact of molecular crowding on the diffusion of membrane proteins has not been studied systematically in a natural system. The diversity of the membrane proteome of most cells may preclude systematic studies. African trypanosomes, however, feature a uniform surface coat that is dominated by a single type of variant surface glycoprotein (VSG). Here we study the density-dependence of the diffusion of different glycosylphosphatidylinositol-anchored VSG-types on living cells and in artificial membranes. Our results suggest that a specific molecular crowding threshold (MCT) limits diffusion and hence affects protein function. Obstacles in the form of heterologous proteins compromise the diffusion coefficient and the MCT. The trypanosome VSG-coat operates very close to its MCT. Importantly, our experiments show that N-linked glycans act as molecular insulators that reduce retarding intermolecular interactions allowing membrane proteins to function correctly even when densely packed.

収録刊行物

• Nature Communications

  Nature Communications 7 2016-09-19

  Springer Nature America, Inc

詳細情報

• CRID: 1050564288162460800
• NII論文ID: 120006540182
• ISSN: 20411723
• HANDLE: 2433/235332
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles