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

Andreas J. W. Hartel, Marius Glogger, Nicola G. Jones, Wasim Abuillan, Christopher Batram, Anne Hermann, Susanne F. Fenz, Motomu Tanaka and Markus Engstler ()
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Andreas J. W. Hartel: Theodor-Boveri-Institute, Biocenter, University of Würzburg
Marius Glogger: Theodor-Boveri-Institute, Biocenter, University of Würzburg
Nicola G. Jones: Theodor-Boveri-Institute, Biocenter, University of Würzburg
Wasim Abuillan: Physical Chemistry of Biosystems, Institute of Physical Chemistry, University of Heidelberg
Christopher Batram: Theodor-Boveri-Institute, Biocenter, University of Würzburg
Anne Hermann: Theodor-Boveri-Institute, Biocenter, University of Würzburg
Susanne F. Fenz: Theodor-Boveri-Institute, Biocenter, University of Würzburg
Motomu Tanaka: Physical Chemistry of Biosystems, Institute of Physical Chemistry, University of Heidelberg
Markus Engstler: Theodor-Boveri-Institute, Biocenter, University of Würzburg

Nature Communications, 2016, vol. 7, issue 1, 1-9

Abstract: Abstract 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.

Date: 2016
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DOI: 10.1038/ncomms12870

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