Proteomics

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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. Stable 18O-ATP labeled kinase assay linked phospho-proteomics (SIKALIP) identifies a collection of putative Mast2 substrate. Our results develop a biochemical profile of the MAST Kinases, provide insight into their regulatory mechanisms, and begin to identify the cellular functionof MAST2.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Michael Lemke Lemke  

LAB HEAD: Thurl Eugene

PROVIDER: PXD069171 | Pride | 2026-01-05

REPOSITORIES: Pride

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20220908_MC_DPQE_MAST2_01_XJ04_11.raw Raw
20220908_MC_DPQE_MAST2_02_XJ04_11.raw Raw
20221013_MC_DPQE_MAST2_01_MC21_21.raw Raw
20221013_MC_DPQE_MAST2_02_MC21_21.raw Raw
202311117_MAST2_1.mzML Mzml
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Publications

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  ...[more]

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