Mint 3: A ubiquitous mint isoform that does not bind to munc18-1 or -2

被引:69
作者
Okamoto, M
Sudhof, TC
机构
[1] Univ Texas, SW Med Ctr, SW Med Sch, Ctr Basic Neurosci,Howard Hughes Med Inst, Dallas, TX 75235 USA
[2] Univ Texas, SW Med Sch, Dept Mol Genet, Dallas, TX 75235 USA
关键词
exocytosis; PTB domain; PDZ domain; mint; membrane traffic; Alzheimer's precursor protein (APP);
D O I
10.1016/S0171-9335(98)80103-9
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Mint 1 and 2 are proteins that bind to munc18-1, an essential component of the synaptic vesicle fusion machinery, and are detectably expressed only in neurons [Okamoto and Sudhof, J. Biol, Chem, 272, 31459-31464 (1997)]. Mint 1 and 2 are composed of a variable N-terminal region that includes a conserved munc18-1-binding site, and a constant C-terminal region that contains one PTB and two PDZ domains. We have now identified a third mint isoform, mint 3. Similar to mint 1 and 2, the C-terminal half of mint 3 is composed of one PTB domain and two PDZ domains, However, in contrast to mint 1 and 2, mint 3 lacks an N-terminal munc18-binding domain and does not interact with munc18-1 in yeast two-hybrid assays. Mint 3 is ubiquitously expressed in all tissues, with lowest levels in brain and testis whereas mint 1 and 2 appear to be brain-specific. Our data suggest that mints form a diverse family of proteins with specialized neuronal and ubiquitous isoforms.
引用
收藏
页码:161 / 165
页数:5
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