Genomic organization, chromosomal localization, alternative splicing, and isoforms of the human synaptosome-associated protein-23 gene implicated in vesicle-membrane fusion processes

• Published in: Human genetics 2001-03, Vol.108 (3), p.211-215
• Main Authors: LAZO, Pedro A, NADAL, Marga, FERRER, Milagros, AREA, Estela, HERNANDEZ-TORRES, Javier, NABOKINA, Svetlana M, MOLLINEDO, Faustino, ESTIVILL, Xavier
• Format: Article
• Language: English
• Subjects: Alternative Splicing; Biological and medical sciences; Carrier Proteins - genetics; Carrier Proteins - metabolism; Chromosome Mapping; Chromosomes, Human, Pair 15 - genetics; Cloning, Molecular; Cytoplasmic Vesicles - physiology; DNA - chemistry; DNA - genetics; DNA, Complementary - chemistry; DNA, Complementary - genetics; Exons; Fundamental and applied biological sciences. Psychology; Genes - genetics; Genes. Genome; HeLa Cells; Humans; In Situ Hybridization, Fluorescence; Introns; Membrane Fusion; Membrane Proteins - metabolism; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Protein Binding; Protein Isoforms - genetics; Protein Isoforms - metabolism; Qa-SNARE Proteins; Qb-SNARE Proteins; Qc-SNARE Proteins; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Sequence Analysis, DNA
• ISSN: 0340-6717; 1432-1203
• DOI: 10.1007/s004390100480

Synaptosome-associated protein-23 (SNAP23) is a component of the cellular mechanism required for specific membrane fusion and targetting of intracellular vesicles. We have cloned the full-length human cDNA and the SNAP23 gene. The SNAP23 gene has eight exons, with the initiation codon located in exon 2, and maps to the human chromosome 15q21-22 region. The human SNAP23 gene can generate two types of message, the full-length message (SNAP23A) and a shorter message (SNAP23B). The latter is the result of alternative splicing where exon 5 is joined to exon 7 and the skipping of exon 6; it thus lacks a region that is required for non-specific binding to plasma membranes. The two isoforms, expressed as fusion proteins with glutathione-S-transferase, interact in vitro with human syntaxin 6, thus retaining the specific protein interaction required for membrane fusion. Alterations in the SNAP23 gene might be involved in neurological and other diseases with defects in vesicle-membrane fusion processes that map to 15q15-21.