Protein kinase termed death-associated protein kinase 2 (DAPK2) dependant on calcium/calmodulin (Ca2+/CaM) contains an N-terminal protein kinase domain followed by a conserved CaM-binding domain with significant homologies to those of DAP kinase, a protein kinase involved in apoptosis. Overexpression of DAPK2 significantly induced the morphological changes characteristic of apoptosis. Results indicate that DAPK2 is an additional member of DAP kinase family involved in apoptotic signaling (1). The region of homology spans the catalytic domain and the CaM-regulatory region, whereas the remaining C-terminal part of the protein differs completely from DAP kinase and displays no homology to any known protein. The catalytic domain is also homologous to the recently identified ZIP kinase and to a lesser extent to the catalytic domains of DRAK1 and -2 (2). DAPK2 has a novel regulatory mechanism that controls its pro-apoptotic functions. It comprises a single autophosphorylation event mapped to Ser308 within the CaM regulatory domain. A negative charge at this site reduces both the binding to CaM and the formation of DRP-1 homodimers (3).
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