Journal article

Interactions of Visinin-like Proteins with Phospho-inositides

Karl-Heinz Braunewell, Blessy Paul, Wassim Altarche-Xifro, Cornelia Noack, Kristian Lange, Andreas Hofmann

Australian Journal of Chemistry | CSIRO PUBLISHING | Published : 2010

Abstract

The subcellular membrane localization of neuronal calcium sensor (NCS) proteins in living cells, such as Visinin-like Proteins-1 (VILIP-1) and VILIP-3, differs substantially. We have followed the hypothesis that the differential localization may be due to the specific binding capabilities of individual VILIPs for phosphatidylinositol phosphates (PIPs). Several highly conserved lysine residues in the N-terminal region could provide favourable electrostatic interactions. Molecular modelling results support a binding site for phospho-inositides in the N-terminal area of VILIP-1, and the involvement of the conserved N-terminal lysine residues in binding the phospho-inositol head group. Experimen..

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University of Melbourne Researchers

Grants

Awarded by Deutsche Forschungsgemeinschaft


Funding Acknowledgements

We gratefully acknowledge funding by Fundacao Bial, the European League Against Rheumatism (EULAR), and the Rebecca L Cooper Foundation to A. H., and funding by Deutsche Forschungsgemeinschaft to K.-H. B. (DFG Br-1579/8-1, Priority Program of the German Research Foundation, SPP1226 'Nicotine', GRK 1123). Blessy Paul is recipient of a Griffith University International Research Scholarship. Wassim Altarche-Xifro is a qualifying student in the GRK program 1123 of the DFG.