Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.

The neuronal calcium sensor proteins Visinin-like Proteins 1 (VILIP-1) and 3 (VILIP-3) are effectors of guanylyl cyclase and acetyl choline receptors, and transduce calcium signals in the brain. The "calcium-myristoyl" switch, which involves a post-translationally added myristoyl moiety an...

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Autores principales:	Samuel Rebaud, Anne Simon, Conan K Wang, Lyndel Mason, Loïc Blum, Andreas Hofmann, Agnès Girard-Egrot
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fc5b55b020484fd4867952d9ac9d9769
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spelling	oai:doaj.org-article:fc5b55b020484fd4867952d9ac9d97692021-11-18T08:25:03ZComparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.1932-620310.1371/journal.pone.0093948https://doaj.org/article/fc5b55b020484fd4867952d9ac9d97692014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24699524/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The neuronal calcium sensor proteins Visinin-like Proteins 1 (VILIP-1) and 3 (VILIP-3) are effectors of guanylyl cyclase and acetyl choline receptors, and transduce calcium signals in the brain. The "calcium-myristoyl" switch, which involves a post-translationally added myristoyl moiety and calcium binding, is thought to regulate their membrane binding capacity and therefore, play a critical role in their mechanism of action. In the present study, we investigated the effect of membrane composition and solvent conditions on the membrane binding mechanisms of both VILIPs using lipid monolayers at the air/buffer interface. Results based on comparison of the adsorption kinetics of the myristoylated and non-myristoylated proteins confirm the pivotal role of calcium and the exposed myristol moiety for sustaining the membrane-bound state of both VILIPs. However, we also observed binding of both VILIP proteins in the absence of calcium and/or myristoyl conjugation. We propose a two-stage membrane binding mechanism for VILIP-1 and VILIP-3 whereby the proteins are initially attracted to the membrane surface by electrostatic interactions and possibly by specific interactions with highly negatively charged lipids head groups. The extrusion of the conjugated myristoyl group, and the subsequent anchoring in the membrane constitutes the second stage of the binding mechanism, and ensures the sustained membrane-bound form of these proteins.Samuel RebaudAnne SimonConan K WangLyndel MasonLoïc BlumAndreas HofmannAgnès Girard-EgrotPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 4, p e93948 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Samuel Rebaud Anne Simon Conan K Wang Lyndel Mason Loïc Blum Andreas Hofmann Agnès Girard-Egrot Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.
description	The neuronal calcium sensor proteins Visinin-like Proteins 1 (VILIP-1) and 3 (VILIP-3) are effectors of guanylyl cyclase and acetyl choline receptors, and transduce calcium signals in the brain. The "calcium-myristoyl" switch, which involves a post-translationally added myristoyl moiety and calcium binding, is thought to regulate their membrane binding capacity and therefore, play a critical role in their mechanism of action. In the present study, we investigated the effect of membrane composition and solvent conditions on the membrane binding mechanisms of both VILIPs using lipid monolayers at the air/buffer interface. Results based on comparison of the adsorption kinetics of the myristoylated and non-myristoylated proteins confirm the pivotal role of calcium and the exposed myristol moiety for sustaining the membrane-bound state of both VILIPs. However, we also observed binding of both VILIP proteins in the absence of calcium and/or myristoyl conjugation. We propose a two-stage membrane binding mechanism for VILIP-1 and VILIP-3 whereby the proteins are initially attracted to the membrane surface by electrostatic interactions and possibly by specific interactions with highly negatively charged lipids head groups. The extrusion of the conjugated myristoyl group, and the subsequent anchoring in the membrane constitutes the second stage of the binding mechanism, and ensures the sustained membrane-bound form of these proteins.
format	article
author	Samuel Rebaud Anne Simon Conan K Wang Lyndel Mason Loïc Blum Andreas Hofmann Agnès Girard-Egrot
author_facet	Samuel Rebaud Anne Simon Conan K Wang Lyndel Mason Loïc Blum Andreas Hofmann Agnès Girard-Egrot
author_sort	Samuel Rebaud
title	Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.
title_short	Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.
title_full	Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.
title_fullStr	Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.
title_full_unstemmed	Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.
title_sort	comparison of vilip-1 and vilip-3 binding to phospholipid monolayers.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/fc5b55b020484fd4867952d9ac9d9769
work_keys_str_mv	AT samuelrebaud comparisonofvilip1andvilip3bindingtophospholipidmonolayers AT annesimon comparisonofvilip1andvilip3bindingtophospholipidmonolayers AT conankwang comparisonofvilip1andvilip3bindingtophospholipidmonolayers AT lyndelmason comparisonofvilip1andvilip3bindingtophospholipidmonolayers AT loicblum comparisonofvilip1andvilip3bindingtophospholipidmonolayers AT andreashofmann comparisonofvilip1andvilip3bindingtophospholipidmonolayers AT agnesgirardegrot comparisonofvilip1andvilip3bindingtophospholipidmonolayers
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Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.

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