Journal article
Specific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins
S Rebaud, CK Wang, J Sarkis, L Mason, A Simon, LJ Blum, A Hofmann, AP Girard-Egrot
Biochimica Et Biophysica Acta Biomembranes | 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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Awarded by National Health and Medical Research Council
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).