Characterization of Mast2 kinase defines structural features, regulation, and substrates.

ABSTRACT: The mammalian microtubule-associated serine/threonine (MAST) kinases are a highly conserved subfamily of AGC kinases that are implicated as therapeutic targets for cancer and diabetes. However, the activity, regulation, and substrates of MAST kinases are poorly understood. We examined the biochemical activity of Mast2, as a representative of the MAST family. The domain of unknown function (DUF1908) is necessary for Mast2 kinase activity in vitro, while the PDZ domain is dispensable. Mast2 kinase activity does not appear to be compatible with the AGC kinase model of T-loop phospho-activation. Instead, it contains a unique insertion that is likely stabilized by ion-pair interactions. The C terminus of the kinase domain contains motifs regulated by mechanistic target of rapamycin (mTOR) in ot

SUBMITTER: Lemke MC 

PROVIDER: S-EPMC12732324 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature