DAPK3 or Death-associated protein kinase 3 (also known as ZIP) plays a role in apoptosis (1). DAPK3 is a nuclear serine/threonine-specific kinase that phosphorylates core histones H3 and H4, and myosine light chain in vitro. DAPK3 interacts with transcription and splicing factors as well as with pro-apoptotic protein Par-4 suggesting that it participates in multiple cellular processes. DAPK3 contains a leucine zipper structure at its C terminus and this region is responsible for binding to ATF4. The leucine zipper domain is necessary for the homodimerization of DAPK3 as well as for the activation of the kinase (2).
ZIP, ZIPK, FLJ36473
1. Kawai, T. et al: ZIP kinase, a novel serine/threonine kinase which mediates apoptosis. Mol. Cell Biol. 1998;18(3):1642-51.
2. Preuss, U. et al. Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase. Nucleic Acids Res. 2003; 31(3):878-85.
Sample Kinase Activity Plot. For specific information on a given lot, see related technical data sheet.
Sample Purity Data. For specific information on a given lot, see related technical data sheet.
Storage, Stability and Shipping:
Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
Mor I et al., Death-associated protein kinase increases glycolytic rate through binding and activation of pyruvate kinase Oncogene February 2012 10.1038/onc.2011.264
N Fujiwara et al., Regulation of Beclin 1 Protein Phosphorylation and Autophagy by Protein Phosphatase 2A (PP2A) and Death-associated Protein Kinase 3 (DAPK3). Journal of Biological Chemistry May 2016 10.1074/jbc.M115.704908
Apoptosis/Autophagy, Cancer, Cellular Stress, ERK/MAPK Pathway, Inflammation, Neurobiology, Ser/Thr Kinases