Disease relevance of STK17B

• The purified CHP and rat DRAK2 proteins synthesized in Escherichia coli could bind in vitro [1].

High impact information on STK17B

• Transgenic drak2 overexpression in mice leads to increased T cell apoptosis and compromised memory T cell development [2].
• 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 [3].
• 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 [3].
• Rat DRAK2 is expressed highly in thymus, spleen, and testis, where the apoptosis plays an important role in physiology [1].
• Overexpression of the rat homologue of DRAK2 caused apoptosis-like cell death of NIH3T3 cells, which was dependent on the kinase activity, confirming the previous result for DRAK2 [1].

Associations of STK17B with chemical compounds

• This increase in phosphorylation was dependent on intracellular calcium mobilization, because BAPTA-AM blocked DRAK2 kinase activity, whereas the SERCA inhibitor thapsigargin promoted Ser(12) phosphorylation [4].

Anatomical context of STK17B

• CHP and rat DRAK2 expressed in COS-7 cells were found to be localized in the Golgi apparatus and nucleus, respectively [1].
• The intracellular location of DRAK2 depended on the cell line: DRAK2 was found primarily in the nuclei of NRK, NIH3T3, and Caco-2 cells while it was present primarily in the cytoplasm of ACL-15, HeLa, and WI-38 cells [5].

Regulatory relationships of STK17B

• DAP kinase-related apoptosis-inducing kinase 2 (DRAK2), a member of the DAP kinase family, is a serine/threonine kinase capable of inducing apoptosis [5].

Other interactions of STK17B

• DRAK1 and DRAK2 show 59.7% identity and display ubiquitous expression [3].

References