Roth D, Morgan A, Burgoyne R D
Physiological Laboratory, University of Liverpool, UK.
FEBS Lett. 1993 Apr 12;320(3):207-10. doi: 10.1016/0014-5793(93)80587-k.
Calcium-dependent secretion in digitonin-permeabilized adrenal chromaffin cells is stimulated by exogenous annexin II and 14-3-3 proteins. These proteins share a conserved domain that has been suggested to be involved in specific protein-protein interactions. We examined whether this domain was involved in secretion by using a synthetic peptide (P16) of sequence KGDYQKALLYLCGGDD corresponding to the C-terminus of annexin II. P16, but not truncated peptides, prevented the stimulation of secretion by 14-3-3 proteins and produced a partial inhibition of control secretion. These data suggest that the shared annexin/14-3-3 domain is important in the mechanisms controlling Ca(2+)-dependent secretion and may play a key role in protein-protein interactions during exocytosis.
在洋地黄皂苷通透处理的肾上腺嗜铬细胞中，钙依赖性分泌受外源膜联蛋白II和14-3-3蛋白的刺激。这些蛋白共享一个保守结构域，有人认为该结构域参与特定的蛋白质-蛋白质相互作用。我们使用与膜联蛋白II C末端对应的序列为KGDYQKALLYLCGGDD的合成肽（P16），研究了该结构域是否参与分泌过程。P16而非截短肽可阻止14-3-3蛋白对分泌的刺激，并对对照分泌产生部分抑制作用。这些数据表明，膜联蛋白/14-3-3共享结构域在控制钙依赖性分泌的机制中很重要，并且可能在胞吐过程中的蛋白质-蛋白质相互作用中起关键作用。
