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Caspase-8 function, and phosphorylation, in cell migration

机译:Caspase-8功能和磷酸化,细胞迁移

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Caspase-8 is involved in a number of cellular functions, with the most well established being the control of cell death. Yet caspase-8 is unique among the caspases in that it acts as an environmental sensor, transducing a range of signals to cells, modulating responses that extend far beyond simple survival. Ranging from the control of apoptosis and necroptosis and gene regulation to cell adhesion and migration, caspase-8 uses proteolytic and non-proteolytic functions to alter cell behavior. Novel interacting partners provide mechanisms for caspase-8 to position itself at signaling nodes that affect a variety of signaling pathways. Here, we examine the catalytic and noncatalytic modes of action by which caspase-8 influences cell adhesion and migration. The mechanisms vary from post-cleavage remodeling of the cytoskeleton to signaling elements that control focal adhesion turnover. This is facilitated by caspase-8 interaction with a host of cell proteins ranging from the proteases caspase-3 and calpain-2 to adaptor proteins such as p85 and Crk, to the Src family of tyrosine kinases. (C) 2018 Published by Elsevier Ltd.
机译:Caspase-8参与了许多细胞功能,具有最多的是对细胞死亡的控制。然而,Caspase-8在胱天蛋白酶中是独特的,因为它充当环境传感器,将一系列信号转换为细胞,调节延伸超出简单存活的反应。从对细胞凋亡和肮脏的控制和基因调节的控制,Caspase-8使用蛋白水解和非蛋白水解功能来改变细胞行为。新型互动伴侣提供了Caspase-8的机制,以在影响各种信令途径的信令节点处定位自身。在这里,我们检查Caspase-8影响细胞粘附和迁移的催化和非催化的作用方式。该机制因细胞骨架的后切割后重组到控制焦粘连周转的信号元件。通过Caspase-8与来自蛋白酶caspase-3和Calpain-2的宿主蛋白质的相互作用的相互作用促进了这一点,以使如P85和Crk等适配器蛋白质到SRC系列酪氨酸激酶。 (c)2018由elestvier有限公司出版

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