An electrostatic switching mechanism to control the lipid transfer activity of Osh6p

An electrostatic switching mechanism to control the lipid transfer activity of Osh6p

Osh6p and Osh7p are yeast lipid transfer proteins (LTPs) that must transiently interact with membranes but how they escape from the electrostatic attraction of the plasma membrane is unclear. Here authors show that Osh6p reduces its avidity for anionic membranes once it captures PS or PI4P, due to a...

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Autores principales: Nicolas-Frédéric Lipp, Romain Gautier, Maud Magdeleine, Maxime Renard, Véronique Albanèse, Alenka Čopič, Guillaume Drin
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/a0889337e6f9452092e32fdc0571b00f
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spelling oai:doaj.org-article:a0889337e6f9452092e32fdc0571b00f2021-12-02T16:57:54ZAn electrostatic switching mechanism to control the lipid transfer activity of Osh6p10.1038/s41467-019-11780-y2041-1723https://doaj.org/article/a0889337e6f9452092e32fdc0571b00f2019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11780-yhttps://doaj.org/toc/2041-1723Osh6p and Osh7p are yeast lipid transfer proteins (LTPs) that must transiently interact with membranes but how they escape from the electrostatic attraction of the plasma membrane is unclear. Here authors show that Osh6p reduces its avidity for anionic membranes once it captures PS or PI4P, due to a molecular lid closing its lipid-binding pocket.Nicolas-Frédéric LippRomain GautierMaud MagdeleineMaxime RenardVéronique AlbanèseAlenka ČopičGuillaume DrinNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-17 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Nicolas-Frédéric Lipp
Romain Gautier
Maud Magdeleine
Maxime Renard
Véronique Albanèse
Alenka Čopič
Guillaume Drin
An electrostatic switching mechanism to control the lipid transfer activity of Osh6p
description Osh6p and Osh7p are yeast lipid transfer proteins (LTPs) that must transiently interact with membranes but how they escape from the electrostatic attraction of the plasma membrane is unclear. Here authors show that Osh6p reduces its avidity for anionic membranes once it captures PS or PI4P, due to a molecular lid closing its lipid-binding pocket.
format article
author Nicolas-Frédéric Lipp
Romain Gautier
Maud Magdeleine
Maxime Renard
Véronique Albanèse
Alenka Čopič
Guillaume Drin
author_facet Nicolas-Frédéric Lipp
Romain Gautier
Maud Magdeleine
Maxime Renard
Véronique Albanèse
Alenka Čopič
Guillaume Drin
author_sort Nicolas-Frédéric Lipp
title An electrostatic switching mechanism to control the lipid transfer activity of Osh6p
title_short An electrostatic switching mechanism to control the lipid transfer activity of Osh6p
title_full An electrostatic switching mechanism to control the lipid transfer activity of Osh6p
title_fullStr An electrostatic switching mechanism to control the lipid transfer activity of Osh6p
title_full_unstemmed An electrostatic switching mechanism to control the lipid transfer activity of Osh6p
title_sort electrostatic switching mechanism to control the lipid transfer activity of osh6p
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/a0889337e6f9452092e32fdc0571b00f
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