Yoo Sungsoo M, Cerione Richard A, Antonyak Marc A
Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA, USA.
Department of Molecular Medicine, Cornell University, Ithaca, NY, USA.
Small GTPases. 2020 Mar;11(2):77-85. doi: 10.1080/21541248.2017.1362496. Epub 2017 Dec 31.
Cool-associated tyrosine phosphorylated protein 1 (Cat1), also referred to as GPCR-kinase interacting protein 1 (Git1), is a ubiquitously expressed, multi-domain protein that is best known for regulating cell shape and migration. Cat1/Git1 functions as a GTPase activating protein (GAP) that inactivates certain members of the ADP-ribosylation factor (Arf) family of small GTPases. It is also a scaffold that brings together several signaling proteins at specific locations within the cell, ensuring their efficient activation. Here we will discuss what is known regarding the classical role of Cat1/Git1 in the regulation of cell morphology and migration, as well as highlight some more recent findings that suggest this interesting signaling/scaffolding protein may also contribute in unexpected ways to oncogenic transformation.
冷相关酪氨酸磷酸化蛋白1(Cat1),也被称为G蛋白偶联受体激酶相互作用蛋白1(Git1),是一种广泛表达的多结构域蛋白,以调节细胞形态和迁移而闻名。Cat1/Git1作为一种GTP酶激活蛋白(GAP),可使小GTP酶的ADP核糖基化因子(Arf)家族的某些成员失活。它也是一种支架蛋白,能在细胞内的特定位置聚集多种信号蛋白,确保它们的有效激活。在这里,我们将讨论关于Cat1/Git1在调节细胞形态和迁移中的经典作用的已知信息,并强调一些最新发现,这些发现表明这种有趣的信号/支架蛋白可能也以意想不到的方式促进致癌转化。