Sudlow A W, McFerran B W, Bodill H, Barnard R J, Morgan A, Burgoyne R D
Physiological Laboratory, University of Liverpool, UK.
FEBS Lett. 1996 Sep 16;393(2-3):185-8. doi: 10.1016/0014-5793(96)00880-0.
Soluble N-ethylmaleimide-sensitive fusion protein attachment proteins (SNAP) proteins function in Ca(2+)-regulated exocytosis. Recent work (Schiavo et al. (1996) Nature 378, 733-736) based on in vitro protein interactions has raised the possibility that alpha- and beta-SNAPs have distinct roles in exocytosis. We have examined this possibility by comparing the activities of recombinant alpha- and beta-SNAPs. Both of these proteins were able to similarly bind NSF and activate its ATPase activity but to a lesser extent than gamma-SNAP. When introduced into digitoninpermeabilised chromaffin cells, both alpha- and beta-SNAP stimulated Ca(2+)-regulated exocytosis in a MgATP-dependent manner. The dose-response relationships for these proteins were essentially the same and addition of both proteins did not lead to any further increase in exocytosis above that due to each protein alone. We conclude that alpha- and beta-SNAPs are interchangeable isoforms with similar functions in regulated exocytosis.
可溶性N - 乙基马来酰亚胺敏感融合蛋白附着蛋白(SNAP)在钙离子调节的胞吐作用中发挥功能。最近基于体外蛋白质相互作用的研究工作(Schiavo等人,《自然》,1996年,第378卷,第733 - 736页)提出α - SNAP和β - SNAP在胞吐作用中可能具有不同作用的可能性。我们通过比较重组α - SNAP和β - SNAP的活性来研究这种可能性。这两种蛋白质都能够同样地结合N - 乙基马来酰亚胺敏感因子(NSF)并激活其ATP酶活性,但程度低于γ - SNAP。当将它们导入洋地黄皂苷通透化的嗜铬细胞时,α - SNAP和β - SNAP都以MgATP依赖的方式刺激钙离子调节的胞吐作用。这些蛋白质的剂量 - 反应关系基本相同,并且同时添加这两种蛋白质并不会导致胞吐作用比单独添加每种蛋白质时进一步增加。我们得出结论,α - SNAP和β - SNAP是在调节性胞吐作用中具有相似功能的可互换同工型。