GRASP: A Multitasking Tether.
GRASP: A Multitasking Tether.
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DOI：
10.3389/fcell.2016.00001
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发表时间：
2016
影响因子：
5.5
通讯作者：
Linstedt AD
中科院分区：
文献类型：
--
作者：
Rabouille C;Linstedt AD
最初在体外鉴定为高尔基堆积因子，高尔基重组堆积蛋白（GRASP）家族已被证明具有多种细胞作用的膜系索。作为对先前对GRASP家族的全面综述的更新（Giuliani et al.,; Vinke et al.,; Jarvela and Linstedt,），我们在这里概述了有关其不同作用的最新发现。最近的晶体结构对grip介导的系固机制有了新的认识。GRASP65和GRASP55系链膜与它们在哺乳动物细胞高尔基带形成和有丝分裂开始时高尔基带解联中的作用直接相关的模型。然而，同样清楚的是，GRASPs在高尔基体之外，在ER和ER出口位点（ERES）发挥作用。此外，该家族的蛋白在细胞应激中表现出其他作用，特别是在介导跨膜蛋白（高尔基旁路）和细胞质蛋白（通过分泌性自噬体）的非常规分泌方面。
Originally identified as Golgi stacking factors in vitro, the Golgi reassembly stacking protein (GRASP) family has been shown to act as membrane tethers with multiple cellular roles. As an update to previous comprehensive reviews of the GRASP family (Giuliani et al.,; Vinke et al.,; Jarvela and Linstedt,), we outline here the latest findings concerning their diverse roles. New insights into the mechanics of GRASP-mediated tethering come from recent crystal structures. The models of how GRASP65 and GRASP55 tether membranes relate directly to their role in Golgi ribbon formation in mammalian cells and the unlinking of the ribbon at the onset of mitosis. However, it is also clear that GRASPs act outside the Golgi with roles at the ER and ER exit sites (ERES). Furthermore, the proteins of this family display other roles upon cellular stress, especially in mediating unconventional secretion of both transmembrane proteins (Golgi bypass) and cytoplasmic proteins (through secretory autophagosomes).