Actin-binding proteins in a postsynaptic preparation: Lasp-1 is a component of central nervous system synapses and dendritic spines
Actin-binding proteins in a postsynaptic preparation: Lasp-1 is a component of central nervous system synapses and dendritic spines
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DOI：
10.1002/jnr.20224
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发表时间：
2004-10-01
影响因子：
4.2
通讯作者：
Colman, DR
中科院分区：
文献类型：
--
作者：
Phillips, GR;Anderson, TR;Colman, DR
中枢神经系统突触是细胞间通讯的复杂场所。识别和表征突触的蛋白质组分将导致更好地理解神经传递和可塑性的机制。我们应用多维蛋白质鉴定技术（MudPIT）纯化，胍溶解突触后馏分，以确定新的突触定位分子。我们确定了几个肌动蛋白相关的蛋白质，已知调节肌动蛋白聚合和控制细胞运动的非神经细胞，以前没有与中枢神经系统突触功能。其中之一是lasp-1，一种与肌动蛋白相关的LIM和含有SH 3结构域的蛋白质。我们发现，lasp-1是强烈表达的中枢神经系统神经元，并集中在突触部位。总的来说，肌动蛋白相关蛋白在突触后密度分数的优势，特别是那些参与肌动蛋白重组，表明有许多模式，突触F-肌动蛋白聚合的状态，因此，突触生理受到影响。(C)2004 Wiley-Liss，Inc.
CNS synapses are complex sites of cell-cell communication. Identification and characterization of the protein components of synapses will lead to a better understanding of the mechanisms of neurotransmission and plasticity. We applied multidimensional protein identification technology (MudPIT) to purified, guanidine-solubilized postsynaptic fractions to identify novel synaptically localized molecules. We identified several actin-associated proteins known to regulate actin polymerization and control cell motility in nonneural cells that have not previously been associated with CNS synaptic function. One of these is lasp-1, an actin-associated LIM and SH3 domain-containing protein. We show that lasp-1 is strongly expressed by CNS neurons and is concentrated at synaptic sites. Overall, the preponderance of actin-associated proteins in postsynaptic density fractions, and specifically those involved in actin reorganization, suggests that there are many modes by which the state of synaptic F-actin polymerization and, hence, synaptic physiology are affected. (C) 2004 Wiley-Liss, Inc.