It has been demonstrated that two Golgi stacking proteins, GRASP55 and GRASP65, self-interact to form trans-oligomers that tether adjacent Golgi membranes into stacks and ribbons in mammalian cells. This ensures proper functioning of the Golgi apparatus in protein trafficking and processing. More recently, GRASP proteins have drawn extensive attention from researchers due to their diverse and essential roles in and out of the Golgi in different organisms. In this review, we summarize their established roles in Golgi structure formation and function under physiological conditions. We then highlight the emerging and divergent roles for individual GRASP proteins, focusing on GRASP65 in cell migration and apoptosis and GRASP55 in unconventional protein secretion and autophagy under stress or pathological conditions.

已经证明，两种高尔基体堆叠蛋白GRASP55和GRASP65自我相互作用形成反式寡聚物，将哺乳动物细胞中相邻的高尔基体膜束缚成堆叠和带状。这确保了高尔基体在蛋白质运输和加工中的正常运作。最近，GRASP 蛋白因其在不同生物体高尔基体内外的多样化和重要作用而引起了研究人员的广泛关注。在这篇综述中，我们总结了它们在生理条件下高尔基体结构形成和功能中的既定作用。然后，我们重点介绍各个 GRASP 蛋白的新兴和不同作用，重点关注 GRASP65 在细胞迁移和凋亡中的作用，以及 GRASP55 在应激或病理条件下非常规蛋白分泌和自噬中的作用。