ArticleBiochemical and biophysical research communications2013
Structural insights into the activation of MST3 by MO25.
Article in Biochemical and biophysical research communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Association ofTranslational cancer research · 2026Article
- Dimerization and autophosphorylation of the MST family of kinases are controlled by the same set of residues.The Biochemical journal · 2023Article
- Molecular mechanisms involved in regulating protein activity and biological function of MST3.Cell division · 2023Review
- Control of Plant Cell Growth and Proliferation by MO25A, a Conserved Major Component of the Mammalian Sterile 20-Like Kinase Pathway.Plant & cell physiology · 2023Article
- NDR kinase tricornered genetically interacts with Ccm3 and metabolic enzymes in Drosophila melanogaster tracheal development.G3 (Bethesda, Md.) · 2023Article
- Review
- Article
- Pharmacological targeting of SPAK kinase in disorders of impaired epithelial transport.Expert opinion on therapeutic targets · 2017Review
- Discovery of Diverse Small-Molecule Inhibitors of Mammalian Sterile20-like Kinase 3 (MST3).ChemMedChem · 2016Article
- Frameshift Mutations of CAB39L, an Activator of LKB1 Tumor Suppressor, in Gastric and Colorectal Cancers.Pathology oncology research : POR · 2016Article
- MST kinases in development and disease.The Journal of cell biology · 2015Review
- Domain-Swapping Switch Point in Ste20 Protein Kinase SPAK.Biochemistry · 2015Article
- Structural and biochemical insights into the activation mechanisms of germinal center kinase OSR1.The Journal of biological chemistry · 2014Article
- Structure of zebrafish MO25.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Cell cycle regulated interaction of a yeast Hippo kinase and its activator MO25/Hym1.PloS one · 2013Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The MO25 scaffolding protein operates as critical regulator of a number of STE20 family protein kinases (e.g. MST and SPAK isoforms) as well as pseudokinases (e.g. STRAD isoforms that play a critical role in activating the LKB1 tumour suppressor). To better understand how MO25 interacts and stimulates the activity of STE20 protein kinases, we determined the crystal structure of MST3 catalytic domain (residues 19-289) in complex with full length MO25β. The structure reveals an intricate web of interactions between MST3 and MO25β that function to stabilise the kinase domain in a closed, active, conformation even in the absence of ATP or an ATP-mimetic inhibitor. The binding mode of MO25β is reminiscent of the mechanism by which MO25α interacts with the pseudokinase STRADα. In particular we identified interface residues Tyr223 of MO25β and Glu58 and Ile71 of MST3 that when mutated prevent activation of MST3 by MO25β. These data provide molecular understanding of the mechanism by which MO25 isoforms regulates the activity of STE20 family protein kinases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.