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The Journal of Neuroscience logoLink to The Journal of Neuroscience
. 1992 Dec 1;12(12):4634–4641. doi: 10.1523/JNEUROSCI.12-12-04634.1992

The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS

DT Hess 1, TM Slater 1, MC Wilson 1, JH Skene 1
PMCID: PMC6575770  PMID: 1281490

Abstract

A conspicuous correlate of the developmental transformation of axonal growth cones to synaptic terminals is a marked increase in synthesis and axonal transport of a methionine-rich, acidic polypeptide of approximately 25 kDa. This polypeptide, designated “super protein” (SuP), is the most prominent species among methionine-labeled proteins conveyed by rapid axonal transport in mature CNS and PNS neurons of warm- and cold-blooded vertebrates. We show here that SuP is identical to SNAP-25, a highly conserved synaptic protein of known primary structure, by immunoprecipitation with anti-SNAP-25 antiserum of SuP labeled with 35S-methionine and transported by retinal ganglion cells of rat and cat. In addition, we show that SNAP-25/SuP is the most prominent species among retinal polypeptides that incorporate 3H- palmitate in vivo, that it is fatty acylated through a hydroxylamine- labile, thioester bond, and that palmitoylated SNAP-25/SuP is axonally transported. Thus, SNAP-25/SuP is a rapidly transported constituent of the presynaptic apparatus and a major neuronal substrate for long-chain fatty acylation.


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