Electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.

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 b...

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Autores principales:	Yuri N Antonenko, Andreas Horner, Peter Pohl
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0ade6c6b1c74483aa4254375a478d822
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spelling	oai:doaj.org-article:0ade6c6b1c74483aa4254375a478d8222021-11-18T08:03:51ZElectrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.1932-620310.1371/journal.pone.0052839https://doaj.org/article/0ade6c6b1c74483aa4254375a478d8222012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23285199/?tool=EBIhttps://doaj.org/toc/1932-6203Protein 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 τ(PLL) of the clustered channels. In contrast, if PLL was bound to only one leaflet, neither D(PLL) nor τ(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.Yuri N AntonenkoAndreas HornerPeter PohlPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 12, p e52839 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yuri N Antonenko Andreas Horner Peter Pohl Electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.
description	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 τ(PLL) of the clustered channels. In contrast, if PLL was bound to only one leaflet, neither D(PLL) nor τ(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.
format	article
author	Yuri N Antonenko Andreas Horner Peter Pohl
author_facet	Yuri N Antonenko Andreas Horner Peter Pohl
author_sort	Yuri N Antonenko
title	Electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.
title_short	Electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.
title_full	Electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.
title_fullStr	Electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.
title_full_unstemmed	Electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.
title_sort	electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/0ade6c6b1c74483aa4254375a478d822
work_keys_str_mv	AT yurinantonenko electrostaticallyinducedrecruitmentofmembranepeptidesintoclustersrequiresligandbindingatbothinterfaces AT andreashorner electrostaticallyinducedrecruitmentofmembranepeptidesintoclustersrequiresligandbindingatbothinterfaces AT peterpohl electrostaticallyinducedrecruitmentofmembranepeptidesintoclustersrequiresligandbindingatbothinterfaces
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Electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces.

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