Neuroligin 1: a splice site-specific ligand for beta-neurexins

Article Abstract:

Neuroligin 1 is a surface protein which functions as the binding site only for beta-neurexins but only if the neurexins do not have an insert in the alternatively spliced sequence of the G domain. Neuroligin 1 is present at the posterior side of the synapses and contains an extracellular domain, a transmembrane region and a cytoplasmic tail. The interactions of neuroligin 1 and beta-neurexins increase the specificity of interactions of neurons in the brain.

Research, Cell membranes, Plasma membranes, Nerve proteins, Nerve tissue proteins, Cellular recognition

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Complexins: cytosolic proteins that regulate SNAP receptor function

Article Abstract:

Complexins, which are cytosolic proteins present in high concentration in neurons, control soluble N-ethylmaleimide-sensitive factor attachment proteins (SNAP) receptor binding during membrane fusion. Binding of SNAP receptor-core complex, containing syntaxin, synaptobrevin and SNAP-25 molecules, to complexins is very strong. Complexins do not bind to synaptobrevin and SNAP-25, and bind only weakly to syntaxin.

Carrier proteins, Transport proteins, Membrane fusion

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Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold

Article Abstract:

The three-dimensional structure of the first C2 domain of synaptotagmin I at 1.9 angstrom resolution in both Ca2+-bound and Ca2+-free forms has an eight-stranded beta-sandwich constructed around a conserved four-stranded motif called the C2 key. Synaptotagmin I is a synaptic vesicle membrane protein that functions as the Ca2+ sensor in exocytosis. It contains two C2 domains, regulatory sequence motifs.

Analysis, Calcium ions, Proteins, Polypeptides, Protein structure

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