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

被引：12

作者：

Connell, Emma ^{[1
]}

Darios, Frederic ^{[1
]}

Peak-Chew, Sew ^{[1
]}

Soloviev, Mikhail ^{[2
]}

Davletov, Bazbek ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

[2] Royal Holloway Univ London, Sch Biol Sci, Egham TW20 0EX, Surrey, England

来源：

BIOCHEMISTRY | 2009年 / 48卷 / 40期

基金：

英国医学研究理事会;

关键词：

SYNAPTOSOMAL-ASSOCIATED PROTEIN; NEUROTOXIN SEROTYPE-A; T-SNARE SNAP-25; PLASMA-MEMBRANE; DIFFERENTIAL PHOSPHORYLATION; BOTULINUM NEUROTOXINS; EUKARYOTIC PROTEINS; CYTOSOLIC PROTEINS; ESCHERICHIA-COLI; TAGGED PROTEINS;

D O I：

10.1021/bi9012403

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The monoclonal antibody SMI81 binds SNAP-25, a major player in neurotransmitter release, with high affinity and has previously been used to follow changes in the levels of this protein in neuropsychiatric disorders. We report here that the SMI81 epitope is present at the extreme N-terminus of SNAP-25 and, unusually, cannot be recognized when present as an internal sequence. Although it is known that SNAP-25 can be palmitoylated and phosphorylated in brain, we now reveal the existence of a third modification, acetylation of the N-terminus. This acetylation event greatly increases the efficiency of SMI81 antibody binding. We show that this highly specific antibody can be used for studying brain function in many vertebrate organisms.

引用

页码：9582 / 9589

页数：8

共 46 条

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