Regensburg 2010 – wissenschaftliches Programm

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BP: Fachverband Biologische Physik

BP 19: Membranes and Vesicles

BP 19.10: Vortrag

Mittwoch, 24. März 2010, 12:30–12:45, H43

Mesoscopic simulations of membrane protein trafficking and signal transduction across membranes — •Diana Morozova, Gernot Guigas, and Matthias Weiss — DKFZ, Cellular Biophysics Group, Im Neuenheimer Feld 280, D-69120 Heidelberg

Acylation is a frequent posttranslational modification that triggers the membrane association of soluble proteins. Besides those peripheral membrane proteins (PMPs) also many transmembrane proteins are subject to lipid modifications, hence indicating that these membrane anchors may also regulate the trafficking of transmembrane proteins. Using coarse-grained membrane simulations we find that acylation indeed significantly alters the tilting of transmembrane proteins with respect to the bilayer normal. Cluster formation and partitioning behavior due to hydrophobic mismatching with the surrounding lipid bilayer is also altered, therefore allowing for ample possibilities to regulate the trafficking of transmembrane proteins via palmitoylation [1].

Using the same simulation approach, we also have studied the trafficking of peripheral membrane proteins (PMPs). In particular, we have observed a cross-leaflet oligomerization of PMPs due to membrane mediated attraction. The strength of this effect is determined by the radii and membrane anchor lengths of the involved PMPs. Since both of these might be altered, for example by ligand binding, the observed cross-leaflet oligomerization may be the fundamental process by which PMPs can trigger an intracellular signalling cascade without the need for accessory transmembrane factors.

[1] D. Morozova & M. Weiss, Biophys. J., in press