Jennings Martin D, Pavitt Graham D
Faculty of Life Sciences; The University of Manchester; Manchester UK.
Small GTPases. 2010 Sep;1(2):118-123. doi: 10.4161/sgtp.1.2.13783.
We recently showed in a publication in Nature that the eukaryotic translation initiation factor eIF5 has a second regulatory function and is a GDI (GDP dissociation inhibitor) in addition to its previously characterized role as a GAP (GTPase accelerating protein). These findings provide new insight into the mechanism of translation initiation in eukaryotic cells. Additional findings show that the GDI function is critical for the normal regulation of protein synthesis by phosphorylation of eIF2α at ser51. Because eIF2 phosphorylation is a ubiquitous mode of translational control these results are of broad interest. Here we review these and related studies and suggest they offer further evidence of parallels between the functions of regulators of the translation factor eIF 2 and both heterotrimeric and small GTPases.
我们最近在《自然》杂志上发表的一篇论文中指出,真核生物翻译起始因子eIF5除了其先前已被描述的作为GAP(GTP酶加速蛋白)的作用外,还具有第二种调节功能,并且是一种GDI(GDP解离抑制剂)。这些发现为真核细胞中翻译起始的机制提供了新的见解。其他研究结果表明,GDI功能对于通过ser51位点的eIF2α磷酸化来正常调节蛋白质合成至关重要。由于eIF2磷酸化是翻译控制的一种普遍模式,因此这些结果具有广泛的意义。在这里,我们综述这些以及相关研究,并表明它们进一步证明了翻译因子eIF 2的调节因子的功能与异源三聚体GTP酶和小GTP酶之间存在相似之处。