Journal
PLOS ONE
Volume 7, Issue 12, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0052839
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Funding
- Upper Austrian government
- Austrian Science Fund [W1201]
- Russian Foundation for Basic Research [09-04-00890]
- Russian-Austria exchange program of the OAAD [15/2006]
- Johannes Kepler University
- Austrian Science Fund (FWF) [W1201] Funding Source: Austrian Science Fund (FWF)
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Protein recruitment to specific membrane locations may be governed or facilitated by electrostatic attraction, which originates from a multivalent ligand. Here we explored the energetics of a model system in which this simple electrostatic recruitment mechanism failed. That is, basic poly-L-lysine binding to one leaflet of a planar lipid bilayer did not recruit the triply-charged peptide (O-Pyromellitylgramicidin). Clustering was only observed in cases where PLL was bound to both channel ends. Clustering was indicated (i) by the decreased diffusional PLL mobility D-PLL and (ii) by an increased lifetime tau(PLL) of the clustered channels. In contrast, if PLL was bound to only one leaflet, neither D-PLL nor tau(P) changed. Simple calculations suggest that electrostatic repulsion of the unbound ends prevented neighboring OPg dimers from approaching each other. We believe that a similar mechanism may also operate in cell signaling and that it may e. g. contribute to the controversial results obtained for the ligand driven dimerization of G protein-coupled receptors.
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