Ontology highlight
ABSTRACT:
SUBMITTER: Widau RC
PROVIDER: S-EPMC2859546 | biostudies-literature | 2010 Apr
REPOSITORIES: biostudies-literature
Widau Ryan C RC Jin Yijun Y Dixon Shelley A SA Wadzinski Brian E BE Gallagher Patricia J PJ
The Journal of biological chemistry 20100310 18
The tumor suppressor, death-associated protein kinase (DAPK), is a Ca(2+)/calmodulin-regulated Ser/Thr kinase with an important role in regulating cytoskeletal dynamics. Autophosphorylation within the calmodulin-binding domain at Ser-308 inhibits DAPK catalytic activity. Dephosphorylation of Ser-308 by a previously unknown phosphatase enhances kinase activity and proteasome-mediated degradation of DAPK. In these studies, we identified two holoenzyme forms of protein phosphatase 2A (PP2A), ABalph ...[more]