Sunday, 4 September 2016 to Wednesday, 7 September 2016
Schedule : Back to Mr Marius Glogger
Poster
128

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

Authors

M Glogger3A Hartel3; N Jones3; W Abuillan1; C Batram3; A Hermann3; S Fenz3; M Tanaka2; M Engstler3
1 Lehrstuhl für Physikalische Chemie von Biosystemen, Institut für Physikalische Chemie, Germany;  2 Lehrstuhl für Physikalische Chemie von Biosystemen, Institut für Physikalische Chemie; Institute for Integrated Cell-Material Science (WPI iCeMS), Kyoto University), Germany;  3 Lehrstuhl für Zell- und Entwicklungsbiologie, Biozentrum der Universität Würzburg, Germany

Discussion

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 GPI-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.

Schedule

Hosted By

British Society for Parasitology (BSP)

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