Differential expression of two novel Munc13 proteins in rat brain

• Published in: Biochemical journal Vol. 337 ( Pt 3); no. 3; pp. 363 - 371
• Main Authors: Augustin, I, Betz, A, Herrmann, C, Jo, T, Brose, N
• Format: Journal Article
• Language: English
• Published: England 01.02.1999
• Subjects: Amino Acid Sequence; Animals; Brain - metabolism; In Situ Hybridization; Intracellular Signaling Peptides and Proteins; Male; Membrane Proteins - metabolism; Mice; Molecular Sequence Data; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - metabolism; Organ Specificity; Qa-SNARE Proteins; Rats; Rats, Wistar; RNA, Messenger - metabolism; Subcellular Fractions - metabolism
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/0264-6021:3370363

Munc13-1, a mammalian homologue of Caenorhabditis elegans unc-13p, is a presynaptic phorbol ester receptor that enhances neurotransmitter release. In the present study we analysed the regional, cellular and subcellular expression patterns in rat of two novel Munc13 proteins, Munc13-2 and Munc13-3. We demonstrate by hybridization in situ that Munc13-1 mRNA is expressed throughout the brain, whereas Munc13-2 mRNA is preferentially present in rostral brain regions, and Munc13-3 mRNA in caudal areas. In an analysis of subcellular brain fractions with isoform-specific antibodies, we show that the novel Munc13 proteins are enriched in synapses. Immunocytochemical examination of rat cerebellar sections indicates that Munc13-3, like Munc13-1, is concentrated in presynaptic terminals. Our results characterize Munc13 proteins as a family of neuron-specific, synaptic molecules that bind to syntaxin, an essential mediator of neurotransmitter release. Munc13-2 and Munc13-3 are expressed in a complementary fashion and might act in concert with Munc13-1 to modulate neurotransmitter release.