N-glycosylation enables high lateral mobility of GPI-anchored proteins at a molecular crowding threshold
Please always quote using this URN: urn:nbn:de:bvb:20-opus-171368
- 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 onThe 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.…
Author: | Andreas J.W. Hartel, Marius Glogger, Nicola G. Jones, Wasim Abuillan, Christopher Batram, Anne Hermann, Susanne F. Fenz, Motomu Tanaka, Markus Engstler |
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URN: | urn:nbn:de:bvb:20-opus-171368 |
Document Type: | Journal article |
Faculties: | Fakultät für Biologie / Theodor-Boveri-Institut für Biowissenschaften |
Language: | English |
Parent Title (English): | Nature Communications |
Year of Completion: | 2016 |
Volume: | 7 |
Article Number: | 12870 |
Source: | Nature Communications 2016, 7:12870. DOI: 10.1038/ncomms12870 |
DOI: | https://doi.org/10.1038/ncomms12870 |
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Tag: | cellular imaging; membrane biophysics; parasitology; single-molecule biophysics |
Release Date: | 2020/12/09 |
Licence (German): | CC BY: Creative-Commons-Lizenz: Namensnennung 4.0 International |