CRUK p53 Signal Transduction Laboratories, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, UK.
FEBS J. 2010 Jan;277(1):48-57. doi: 10.1111/j.1742-4658.2009.07411.x. Epub 2009 Oct 26.
Death-associated protein kinase (DAPK) is a stress-regulated protein kinase that mediates a range of processes, including signal-induced cell death and autophagy. Although the kinase domain of DAPK has a range of substrates that mediate its signalling, the additional protein interaction domains of DAPK are relatively ill defined. This review will summarize our current knowledge of the DAPK interactome, the use of peptide aptamers to define novel protein-protein interaction motifs, and how these new protein-protein interactions give insight into DAPK functions in diverse cellular processes, including growth factor signalling, the regulation of autophagy, and its emerging role in the regulation of immune responses.
死亡相关蛋白激酶（DAPK）是一种应激调节蛋白激酶，可介导多种过程，包括信号诱导的细胞死亡和自噬。尽管 DAPK 的激酶结构域具有一系列介导其信号转导的底物，但 DAPK 的其他蛋白相互作用结构域相对定义不明确。本综述将总结我们目前对 DAPK 相互作用组的了解，使用肽适体来定义新的蛋白-蛋白相互作用基序，以及这些新的蛋白-蛋白相互作用如何深入了解 DAPK 在多种细胞过程中的功能，包括生长因子信号转导、自噬的调节及其在免疫反应调节中的新兴作用。
