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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 and calcium...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3974848/ https://www.ncbi.nlm.nih.gov/pubmed/24699524 http://dx.doi.org/10.1371/journal.pone.0093948 |
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author | Rebaud, Samuel Simon, Anne Wang, Conan K. Mason, Lyndel Blum, Loïc Hofmann, Andreas Girard-Egrot, Agnès |
author_facet | Rebaud, Samuel Simon, Anne Wang, Conan K. Mason, Lyndel Blum, Loïc Hofmann, Andreas Girard-Egrot, Agnès |
author_sort | Rebaud, Samuel |
collection | PubMed |
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 | Online Article Text |
id | pubmed-3974848 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-39748482014-04-08 Comparison of VILIP-1 and VILIP-3 Binding to Phospholipid Monolayers Rebaud, Samuel Simon, Anne Wang, Conan K. Mason, Lyndel Blum, Loïc Hofmann, Andreas Girard-Egrot, Agnès PLoS One Research Article 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. Public Library of Science 2014-04-03 /pmc/articles/PMC3974848/ /pubmed/24699524 http://dx.doi.org/10.1371/journal.pone.0093948 Text en © 2014 Rebaud et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Rebaud, Samuel Simon, Anne Wang, Conan K. Mason, Lyndel Blum, Loïc Hofmann, Andreas Girard-Egrot, Agnès Comparison of VILIP-1 and VILIP-3 Binding to Phospholipid Monolayers |
title | 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_short | Comparison of VILIP-1 and VILIP-3 Binding to Phospholipid Monolayers |
title_sort | comparison of vilip-1 and vilip-3 binding to phospholipid monolayers |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3974848/ https://www.ncbi.nlm.nih.gov/pubmed/24699524 http://dx.doi.org/10.1371/journal.pone.0093948 |
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