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The synapsins are a family of proteins that have long been implicated in the regulation of neurotransmitter release at synapses. Specifically, they are thought to be involved in regulating the number of synaptic vesicles available for release via exocytosis at any one time.

Synapsins are encoded by three different genes, synapsin I, II and III, and different neuron terminals will encode different amounts of these; synapsin will make up 1% of total brain protein at any one time.

Current studies suggest the following hypothesis for the role of synapsin: synapsins bind synaptic vesicles to components of the cytoskeleton which prevents them from migrating to the presynaptic membrane and releasing transmitter. During an action potential, synapsins are phosphorylated by Ca2+/calmodulin-dependent protein kinase II, releasing the synaptic vesicles and allowing them to move to the membrane and release their neurotransmitter.

Gene knockout studies in mice (where the mouse is unable to produce synapsin) have had some surprising results. Mice lacking all three synapsins are prone to seizures, and experience learning defects [1]. These results suggest that while synapsins are not essential for synaptic function, they do serve an important modulatory role. Conversely, studies using transgenic mice in which neuronal signaling is abolished in specific circuitries showed that synaptic activity regulates, but is not essential to maintain, the expression of these proteins [2].

References Edit

  1. Rosahl TW, Geppert M, Spillane D, Herz J, Hammer RE, Malenka RC, Sudhof TC (1993). Short-term synaptic plasticity is altered in mice lacking synapsin I. Cell 75: 661–670.
  2. Kihara AH, Santos TO, Paschon V, Matos RJ, Britto LR (2008). Lack of photoreceptor signaling alters the expression of specific synaptic proteins in the retina. Neuroscience 151: 995–1005.

Template:Nerve tissue protein

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