Donnelly S R, Moss S E
Department of Physiology, University College London, UK.
Cell Mol Life Sci. 1997 Jun;53(6):533-8. doi: 10.1007/s000180050068.
Among the multiplicity of roles suggested for proteins of the annexin family, those implicating these proteins in regulated exocytosis remain among the most convincing. Studies in this area of annexin biology have focused on annexin II, which because of its unusually low Ca(2+)-requirement for phospholipid-binding has many of the requisite properties of a membrane fusogenic Ca2+ sensor. Other annexins are also good candidates for exocytotic mediators, especially annexins I and VII, which have strong vesicle-aggregating activities. In contrast, annexin VI appears to block vesicle aggregation, perhaps acting as a negative regulator of exocytosis. In this review, we consider the evidence for and against annexins having functions in the secretory pathway.
在膜联蛋白家族蛋白质所具有的众多功能中，那些认为这些蛋白质参与调节性胞吐作用的功能仍然是最有说服力的。膜联蛋白生物学这一领域的研究集中在膜联蛋白II上，由于其对磷脂结合的钙离子需求异常低，它具有许多作为膜融合钙离子传感器的必要特性。其他膜联蛋白也是胞吐作用介质的良好候选者，尤其是具有强囊泡聚集活性的膜联蛋白I和VII。相比之下，膜联蛋白VI似乎会阻止囊泡聚集，可能作为胞吐作用的负调节因子发挥作用。在这篇综述中，我们考虑了支持和反对膜联蛋白在分泌途径中发挥作用的证据。
