來自美國(guó)立衛(wèi)生研究院國(guó)家神經(jīng)疾病和中風(fēng)研究院（the National Institute of Neurological Disorders and Stroke），上海交通大學(xué)醫(yī)學(xué)院神經(jīng)學(xué)系等處的研究人員在之前研究的基礎(chǔ)上,，發(fā)現(xiàn)了三種SNARE結(jié)合蛋白之一：Snapin的兩個(gè)重要作用,，這對(duì)于研究突觸小泡融合,，以及融合同步化具有重要意義。這一研究成果公布在Neuron雜志上,。
領(lǐng)導(dǎo)這一研究的是美國(guó)立衛(wèi)生研究院的盛祖杭教授,，其1987年于上海第二醫(yī)科大學(xué)獲醫(yī)學(xué)碩士學(xué)位，2000年被聘為上海第二醫(yī)科大學(xué)神經(jīng)生物學(xué)教研室客座教授,，2001年被聘為二醫(yī)大長(zhǎng)江講座教授,，二醫(yī)大與美國(guó)NIH聯(lián)合培養(yǎng)研究生計(jì)劃的主要策劃者和主持人。
研究人員從Snapin缺陷突變小鼠上分離得到皮層神經(jīng)細(xì)胞,，發(fā)現(xiàn)Snapin能有助于突觸小泡（Synaptic vesicle,，SV）的同時(shí)釋放。而且Snapin缺陷也會(huì)導(dǎo)致EPSCs出現(xiàn)多個(gè)peak,，衰減和裂變時(shí)間增加,，出現(xiàn)無法同步的SV融合。
另外研究人員還發(fā)現(xiàn)Snapin-C66A（SNAP-25和Synaptotagmin二聚體缺陷）的表達(dá)會(huì)減小RRP的大小,，但對(duì)同步融合的影響比較小,，這些研究成果說明Snain具有雙重作用：增強(qiáng)SV的功能，以及調(diào)節(jié)同步SV融合,。（生物谷Bioon.com）
生物谷推薦原始出處：
Neuron, Volume 61, Issue 3, 412-424, 12 February 2009 doi:10.1016/j.neuron.2008.12.029
Snapin Facilitates the Synchronization of Synaptic Vesicle Fusion
Ping-Yue Pan1,2,Jin-Hua Tian1andZu-Hang Sheng1,,
1 Synaptic Function Section, The Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Building 35, Room 3B203, 35 Convent Drive, Bethesda, MD 20892-3701, USA
2 Department of Neurobiology, School of Medicine, Shanghai Jiaotong University, Shanghai 200025, China
Summary
Synaptic vesicle (SV) fusion is a fine-tuned process requiring a concert of fusion machineries. Using cortical neurons from snapin-deficient mice, we reveal a role for Snapin in facilitating synchronous release. In addition to reduced frequency of miniature excitatory postsynaptic currents (mini-EPSCs) and smaller release-ready vesicle pool (RRP) size, snapin deficiency results in EPSCs with multiple peaks and increased rise and decay times, reflecting desynchronized SV fusion. These defects impair both synaptic precision and efficacy during sustained neurotransmission. Transient expression of Snapin not only rescues the slowed kinetics of EPSCs, but also further accelerates the rate found in wild-type neurons. Furthermore, expression of Snapin-C66A, a dimerization-defective mutant with impaired interactions with SNAP-25 and Synaptotagmin, reduces the RRP size but exhibits less effect on synchronized fusion. Our studies provide mechanistic insights into a dual role of Snapin in enhancing the efficacy of SV priming and in fine-tuning synchronous SV fusion.
