Abstract
Death-Associated Protein Kinase 1 (DAPK1) belongs to a family of five serine/threonine (Ser/Thr) kinases that possess tumor suppressive function and also mediate a wide range of cellular processes, including apoptosis and autophagy. The loss and gain-of–function of DAPK1 is associated with various cancer and neurodegenerative diseases respectively. In recent years, mechanistic studies have broadened our knowledge of the molecular mechanisms involved in DAPK1-mediated autophagy/apoptosis. In the present review, we have discussed the structural information and various cellular functions of DAPK1 in a comprehensive manner.
Highlights
Death-Associated Protein Kinase 1 (DAPK1) belongs to a family of five serine/threonine (Ser/Thr) kinases that possess tumor suppressive function and mediate a wide range of cellular processes, including apoptosis and autophagy
Death-associated protein kinase 1 (DAPK1), a part of a family of Ser/Thr kinase, was originally isolated in an unbiased antisense based genetic screen for genes whose protein products were imperative for interferon Gamma (IFN-γ) induced death in HeLa cells (Deiss et al, 1995), and identified by a functional cloning based on its involvement in interferon-γ-induced apoptosis (Bialik and Kimchi, 2006)
DAPK1 is an important regulator of cell death and autophagy which act as a critical component in the ER stress-induced cell death pathway (Gade et al, 2014)
Summary
Death-Associated Protein Kinase 1 (DAPK1) belongs to a family of five serine/threonine (Ser/Thr) kinases that possess tumor suppressive function and mediate a wide range of cellular processes, including apoptosis and autophagy. The ROC-COR domain serves to regulate DAPK1 catalytic activity, but can mediate cellular functions through protein-protein interactions.
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