DRAKs, novel serine/threonine kinases related to death-associated protein kinase that trigger apoptosis.

Article Details

Citation

Sanjo H, Kawai T, Akira S

DRAKs, novel serine/threonine kinases related to death-associated protein kinase that trigger apoptosis.

J Biol Chem. 1998 Oct 30;273(44):29066-71.

PubMed ID
9786912 [ View in PubMed
]
Abstract

The present study describes the cloning of two novel serine/threonine kinases termed DRAK1 and DRAK2, whose catalytic domains are related to that of death-associated protein kinase, a serine/threonine kinase involved in apoptosis. Both DRAKs are composed of the N-terminal catalytic domain and the C-terminal domain that is responsible for regulation of kinase activity. DRAK1 and DRAK2 show 59.7% identity and display ubiquitous expression. An in vitro kinase assay revealed that both DRAKs are autophosphorylated and phosphorylate myosin light chain as an exogenous substrate, although the kinase activity of DRAK2 is significantly lower than that of DRAK1. Both DRAKs are exclusively localized to the nucleus. Furthermore, overexpression of both DRAKs induces the morphological changes of apoptosis in NIH 3T3 cells, suggesting the role of DRAKs in apoptotic signaling.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Serine/threonine-protein kinase 17BO94768Details
Serine/threonine-protein kinase 17AQ9UEE5Details