N-terminal acetylation of the neuronal protein SNAP-25 is revealed by the SMI81 monoclonal antibody. / Connell, Emma; Darios, Frédéric; Peak-Chew, Sew; Soloviev, Mikhail; Davletov, Bazbek.

In: Biochemistry, Vol. 48, No. 40, 2009, p. 9582-9.

Research output: Contribution to journalArticle

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Abstract

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.
Original languageEnglish
Pages9582-9
Number of pages8
JournalBiochemistry
Journal publication date2009
Volume48
Issue40
DOIs
StatePublished

ID: 1384540