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Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C

Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein... NEUROTRANSMITTERS are released at synapses by the Ca2+-regulated exocytosis of synaptic vesicles, which are specialized secretory organelles that store high concentrations of neurotransmitters1,2. The rapid Ca2+-triggered fusion of synaptic vesicles is presumably mediated by specific proteins that must interact with Ca2+ and the phospholipid bilayer. We now report that the cytoplasmic domain of p65, a synaptic vesicle-specific protein3 that binds calmodulin4 contains an internally repeated sequence that is homologous to the regulatory C2-region of protein kinase C (PKC)5. The cytoplasmic domain of recombinant p65 binds acidic phospholipids with a specificity indicating an interaction of p65 with the hydrophobic core as well as the headgroups of the phospholipids. The binding specificity resembles PKC, except that p65 also binds calmodulin, placing the C2-regions in a context of potential Ca2+-regulation that is different from PKC. This is a novel homology between a cellular protein and the regulatory domain of protein kinase C. The structure and properties of p65 suggest that it may have a role in mediating membrane interactions during synaptic vesicle exocytosis. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C

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References (18)

Publisher
Springer Journals
Copyright
Copyright © 1990 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/345260a0
Publisher site
See Article on Publisher Site

Abstract

NEUROTRANSMITTERS are released at synapses by the Ca2+-regulated exocytosis of synaptic vesicles, which are specialized secretory organelles that store high concentrations of neurotransmitters1,2. The rapid Ca2+-triggered fusion of synaptic vesicles is presumably mediated by specific proteins that must interact with Ca2+ and the phospholipid bilayer. We now report that the cytoplasmic domain of p65, a synaptic vesicle-specific protein3 that binds calmodulin4 contains an internally repeated sequence that is homologous to the regulatory C2-region of protein kinase C (PKC)5. The cytoplasmic domain of recombinant p65 binds acidic phospholipids with a specificity indicating an interaction of p65 with the hydrophobic core as well as the headgroups of the phospholipids. The binding specificity resembles PKC, except that p65 also binds calmodulin, placing the C2-regions in a context of potential Ca2+-regulation that is different from PKC. This is a novel homology between a cellular protein and the regulatory domain of protein kinase C. The structure and properties of p65 suggest that it may have a role in mediating membrane interactions during synaptic vesicle exocytosis.

Journal

Nature – Springer Journals

Published: May 17, 1990

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