Abstract
Sorting of transmembrane proteins is a central task of eucaryotic cells, in particular in the secretory pathway.Due to a lack of an organizing mastermind the decision whether a membrane protein participates in secretory transport or not has to be made by a self-organization process on the molecular scale, e.g. via cluster formation. We show by means of coarse-grained membrane simulations that hydrophobic mismatching can drive cluster formation of transmembrane proteins [1]. Also, proteins with different degrees of hydrophobic mismatching can segregate and form homo-oligomers. In addition, we show that proteins partition into the lipid phase with the smallest hydrophobic mismatch if the membrane has a heterogeneous composition. Our data thus indicate that hydrophobic mismatching may help to organize trafficking along the secretory pathway in living cells.[1] U. Schmidt, G. Guigas & M. Weiss, Phys. Rev. Lett. 101, 128104 (2008).
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