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Biochem Biophys Res Commun. 2002 Mar 15;291(5):1232-8.

ATP dependence of the SNARE/caveolin 1 interaction in the hippocampus.

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Department of Physiology and Biophysics, Neuroscience Research Group, University of Calgary, Calgary, Alberta, Canada T2N 4N1.


The molecular mechanisms underlying the regulation of neurotransmission has been an open question for many years. Here, we have examined an interaction between caveolin1 and SNAREs (soluble N-ethylmalemide-sensitive factor attachment protein receptor) which may contribute to the cellular mechanisms underlying changes in synaptic strength. Previously, we reported that application of 4-aminopyridine to hippocampal slices resulted in a persistent potentiation of synaptic transmission and the induction of a short-lasting and specific 40-kDa complex composed of synaptosomal associated protein of 25 kDa (SNAP25) and caveolin1. We have characterized the binding properties of these proteins and observed that in vitro caveolin1 directly associates with both SNAP25 and syntaxin. Caveolin/SNARE interactions are enhanced in the presence of ATP by a mechanism that involves phosphorylation. While caveolin has been associated with cholesterol transport, signal transduction, and transcytosis, this study provides evidence that caveolin is also a SNARE accessory protein.

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