Three splicing variants of tomosyn and identification of their syntaxin-binding region

S Yokoyama, H Shirataki, T Sakisaka… - … and biophysical research …, 1999 - Elsevier
S Yokoyama, H Shirataki, T Sakisaka, Y Takai
Biochemical and biophysical research communications, 1999Elsevier
We have recently isolated a neural tissue-specific syntaxin-1-binding protein, named
tomosyn, which is capable of dissociating Munc18/n-Sec1/rbSec1 from syntaxin-1 to form a
10S tomosyn complex, an intermediate complex converted to the 7S SNARE complex. We
isolated here two splicing variants of tomosyn: one had 36 amino acids (aa) insertion and
another had 17 aa deletion. We named original one m-tomosyn, big one b-tomosyn, and
small one s-tomosyn. s-Tomosyn as well as m-tomosyn was mainly expressed in brain …
We have recently isolated a neural tissue-specific syntaxin-1-binding protein, named tomosyn, which is capable of dissociating Munc18/n-Sec1/rbSec1 from syntaxin-1 to form a 10S tomosyn complex, an intermediate complex converted to the 7S SNARE complex. We isolated here two splicing variants of tomosyn: one had 36 amino acids (aa) insertion and another had 17 aa deletion. We named original one m-tomosyn, big one b-tomosyn, and small one s-tomosyn. s-Tomosyn as well as m-tomosyn was mainly expressed in brain whereas b-tomosyn was ubiquitously expressed. All the isoforms bound to syntaxin-1, but not to syntaxin-2, -3, or -4, and had a region highly homologous to VAMP, another syntaxin-binding protein. This region was necessary but not sufficient for high-affinity binding of tomosyn to syntaxin-1.
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