Journal article

Specific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins

Samuel Rebaud, Conan K Wang, Joe Sarkis, Lyndel Mason, Anne Simon, Loic J Blum, Andreas Hofmann, Agnes P Girard-Egrot

Biochimica et Biophysica Acta-Biomembranes | ELSEVIER | Published : 2014

Abstract

VIsinin-LIke Proteins (VILIPs) are a subfamily of the Neuronal Calcium Sensor (NCS) proteins, which possess both N-myristoylation and EF-hand motifs allowing for a putative 'calcium-myristoyl switch' regulation mechanism. It has previously been established that myristoyl conjugation increases the affinity of proteins for membranes, but, in many cases, a second feature such as a cluster of positively-charged residues is needed for stable membrane binding. The interaction of two members of this family, VILIP-1 and VILIP-3, with Langmuir monolayers as membrane models has been investigated in order to study the effects of both myristoylation and the highly basic region containing conserved poly-..

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University of Melbourne Researchers

Grants

Awarded by National Health and Medical Research Council Early Career Fellowship


Awarded by French Ministry of Higher Education and Research fellowship


Awarded by Fundacao Bial


Funding Acknowledgements

We thank Jeffery Gordon (Washington University, St. Louis) for sharing the pNMT expression plasmid pBB131, and Karl-Heinz Braunewell for providing the cDNA of VILIP-1 and VILIP-3. We thank Christian Salesse for the helpful discussions. Conan K. Wang was supported by a National Health and Medical Research Council Early Career Fellowship (546578). Samuel Rebaud was supported by a French Ministry of Higher Education and Research fellowship (No023/2011-2014). This work was supported in parts by Fundacao Bial (number 09/04) and the Rebecca Cooper Foundation (to Andreas Hofmann).