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

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    Author(s)
    Rebaud, Samuel
    Wang, Conan K
    Sarkis, Joe
    Mason, Lyndel
    Simon, Anne
    Blum, Loic J
    Hofmann, Andreas
    Girard-Egrot, Agnes P
    Griffith University Author(s)
    Hofmann, Andreas
    Mason, Lyndel
    Wang, Conan K.
    Year published
    2014
    Metadata
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    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 ...
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    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-lysine residues on membrane association kinetics and binding properties. Results show that in the presence of calcium, N-myristoylation significantly increases the kinetic rate of VILIP adsorption to the membrane. Additionally, the proteins bind to negatively charged phospholipids independently of the conjugated myristate moiety. Besides the regulatory effect of calcium on the rate of binding presumably due to exposure of the myristoyl moiety ascribed to their putative 'calcium-myristoyl switch', VILIP-1 and -3 also engage specific interactions with biomimetic membranes containing phosphatidylinositol 4,5-bisphosphate (PIP2). The presence of PIP2 increases the membrane association rates of both VILIPs. Taken together, these results show the major kinetic role of N-myristoylation for membrane binding, and highlight the critical role of specific phosphoinositide interactions for membrane association of members of the VILIP family.
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    Journal Title
    Biochimica et Biophysica Acta: international journal of biochemistry and biophysics
    Volume
    1838
    DOI
    https://doi.org/10.1016/j.bbamem.2014.06.021
    Copyright Statement
    © 2014 Elsevier B.V.. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
    Subject
    Biochemistry and cell biology
    Other biological sciences
    Chemical engineering
    Medical parasitology
    Publication URI
    http://hdl.handle.net/10072/64002
    Collection
    • Journal articles

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