Death-associated protein kinase (DAPK) is the inaugural member of a class of Ser/Thr protein kinases whose members exhibit homologous catalytic domains as well as share cell death-associated functions (Bialik and Kimchi 2006). DAPK was discovered by Kimchi and co-workers as a tumor suppressor gene whose expression is lost in multiple tumor types (Cohen and Kimchi 2001). This attracted the interest of several investigators resulting in an impressive body of literature concerning its function, regulation, and involvement in various diseases and conditions. For example, DAPK participates in apoptotic pathways initiated by interferon-γ, TNFα, activated Fas, and loss of attachment to the extracellular matrix (Bialik and Kimchi 2006). By activating p53 in a p19ARF-dependent fashion, DAPK is an intrinsic tumor suppressor that opposes early stage oncogenic transformation (Raveh et al. 2001). However, hypermethylation of...
- Lukas TJ, Mirzoeva S, Watterson DM. Calmodulin-regulated protein kinases. In: Van Eldik LJ, Watterson DM, editors. Calmodulin and signal transduction. New York: Academic; 1998. p. 66–168.Google Scholar