DAPK2

DAPK2, death-associated protein kinase 2, is a calcium/calmodulin-regulated serine/threonine kinase sharing the catalytic and calmodulin-binding architecture of DAPK1 but lacking its long carboxy-terminal extensions and death domain. DAPK2 forms autoinhibited homodimers that are relieved upon calmodulin binding. It phosphorylates myosin regulatory light chain, modulating cytoskeletal dynamics during cell death, and its overexpression induces apoptosis in multiple cell lines, including hematopoietic contexts where DAPK2 expression is prominent. Reduced expression through promoter methylation has been described in several malignancies, consistent with tumor suppressor behavior, and the enzyme has additionally been implicated in granulocytic differentiation, linking death signaling to myeloid lineage decisions.