@article{HartelGloggerJonesetal.2016,
  author    = {Hartel, Andreas J.W. and Glogger, Marius and Jones, Nicola G. and Abuillan, Wasim and Batram, Christopher and Hermann, Anne and Fenz, Susanne F. and Tanaka, Motomu and Engstler, Markus},
  title     = {N-glycosylation enables high lateral mobility of GPI-anchored proteins at a molecular crowding threshold},
  series = {Nature Communications},
  volume    = {7},
  journal   = {Nature Communications},
  doi       = {10.1038/ncomms12870},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-171368},
  year      = {2016},
  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.},
  language  = {en}
}