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- W2083081567 abstract "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 Südhof, 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." @default.
- W2083081567 created "2016-06-24" @default.
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- W2083081567 date "1998-11-01" @default.
- W2083081567 modified "2023-09-27" @default.
- W2083081567 title "Mint 3: A ubiquitous mint isoform that does not bind to munc18-1 or -2" @default.
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- W2083081567 doi "https://doi.org/10.1016/s0171-9335(98)80103-9" @default.
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