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

Article Abstract:

Synaptic vesicles are organelles at the ends of nerves that store neurotransmitters. The release of neurotransmitters is regulated by calcium ions. The synaptic vesicles from different nerves fuse, and neurotransmitters are released; they then can cross the membranes to other nerve cells or to muscles and tendons. The calcium-triggered fusion is thought to occur through specific proteins that interact with both calcium ions and phospholipids, which are present in the membranes of the vesicles. The gene encoding a protein found only in synaptic vesicles, known as p65, which binds calmodulin, a calcium-binding protein, has been isolated. The DNA of the gene has been sequenced, and it contains a sequence that is similar to a portion of the protein kinase C molecule, which is involved in regulation of cellular responses. Protein kinase C is a molecule that participates in many aspects of cell activation. The homology between a cellular protein and the regulatory region of protein kinase C has not been previously seen. The p65 molecule was shown to bind to one particular type of phospholipid, but not another. No binding to calcium ions could be seen. The p65 molecule may be involved in the regulation of the interactions necessary for the release of neurotransmitters from the synaptic vesicles and may do so by binding phospholipids in the membranes of the synaptic vesicle. (Consumer Summary produced by Reliance Medical Information, Inc.)

Genetic aspects, Nerves, Protein kinases

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STED microscopy reveals that synaptotagmin remains clustered after synaptic vesicle exocytosis

Article Abstract:

Synaptic transmission is mediated by neurotransmitters that are stored in synaptic vesicles and released by exocytosis upon activation, then the vesicle membrane is retrieved by endocytosis, and synaptic vesicles are regenerated and re-filled with neurotransmitter. Stimulated emission of depletion is used to reduce the focal spot area by about an order of magnitude below the diffraction limit, thereby resolving individual vesciles in the synapse.

United States, Science & research, Exocytosis

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Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein

Article Abstract:

Constitutive and regulated vesicular pathways appear to use homologous proteins for membrane trafficking, suggesting that the two are closer in evolution and mechanism than once thought. Cellubrevin is a new synaptobrevin analog that appeared in all tissues and cells tested, that is as vulnerable to tetanus toxin as synaptobrevin, and that is a membrane trafficking protein of a constitutively recycling pathway.

Membrane proteins

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