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

Rebaud S., Simon A., Wang C.K., Mason L., Blum L., Hofmann A. and Girard-Egrot A. (2014) Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers. PLoS ONE, 9 4: e93948.1-e93948.8. doi:10.1371/journal.pone.0093948

Author Rebaud S.
Simon A.
Wang C.K.
Mason L.
Blum L.
Hofmann A.
Girard-Egrot A.
Title Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers
Journal name PLoS ONE   Check publisher's open access policy
ISSN 1932-6203
Publication date 2014-04-03
Year available 2014
Sub-type Article (original research)
DOI 10.1371/journal.pone.0093948
Open Access Status DOI
Volume 9
Issue 4
Start page e93948.1
End page e93948.8
Total pages 8
Place of publication San Francisco United States
Publisher Public Library of Science
Language eng
Abstract 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.
Keyword Multidisciplinary Sciences
Science & Technology - Other Topics
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID 37677
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 6 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 5 times in Scopus Article | Citations
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