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N-Terminal Acetylation of the Neuronal Protein SNAP-25 Is Revealed by the SMI81 Monoclonal Antibody

机译:SMI81单克隆抗体揭示了神经元蛋白SNAP-25的N末端乙酰化

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ABSTRACT: Themonoclonal antibody SMI81 binds SNAP-25, amajor player in neurotransmitter release, withnhigh affinity and has previously been used to follow changes in the levels of this protein in neuropsychiatricndisorders. We report here that the SMI81 epitope is present at the extreme N-terminus of SNAP-25 and,nunusually, cannot be recognized when present as an internal sequence. Although it is known that SNAP-25ncan be palmitoylated and phosphorylated in brain, we now reveal the existence of a third modification,nacetylation of the N-terminus. This acetylation event greatly increases the efficiency of SMI81 antibodynbinding.We show that this highly specific antibody can be used for studying brain function inmany vertebratenorganisms.
机译:摘要:单克隆抗体SMI81以高亲和力与SNAP-25结合,SNAP-25是神经递质释放的主要参与者,以前已被用来追踪该蛋白在神经精神疾病中的水平变化。我们在此报告,SMI81表位存在于SNAP-25的极端N端,并且当作为内部序列存在时,通常无法识别。尽管已知SNAP-25n可以在大脑中被棕榈酰化和磷酸化,但我们现在揭示了第三种修饰的存在,即N末端的n乙酰化。这种乙酰化事件大大提高了SMI81抗体结合的效率。我们表明,这种高度特异性的抗体可用于研究许多脊椎动物的脑功能。

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