Kinetic Regulation of the Mammalian Sterile 20-like Kinase 2 (MST2).

ABSTRACT: Canonically, MST1/2 functions as a core kinase of the Hippo pathway and noncanonically during both apoptotic signaling and with RASSFs in T-cells. Faithful signal transduction by MST1/2 relies on both appropriate activation and regulated substrate phosphorylation by the activated kinase. Considerable progress has been made in understanding the molecular mechanisms regulating the activation of MST1/2 and identifying downstream signaling events. Here, we investigated the ability of MST2 to phosphorylate a peptide substrate and how that activity is regulated. Using a steady-state kinetic system, we parse the contribution of different factors to substrate phosphorylation, including the domains of MST2, phosphorylation, caspase cleavage, and complex formation. We found that in the unphosphoryla

SUBMITTER: Koehler TJ 

PROVIDER: S-EPMC10167949 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature