ArticleThe Journal of biological chemistry2020
Biophysical characterization of SARAH domain-mediated multimerization of Hippo pathway complexes in
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- MST2 methylation by PRMT5 inhibits Hippo signaling and promotes pancreatic cancer progression.The EMBO journal · 2023Article
- Dimerization and autophosphorylation of the MST family of kinases are controlled by the same set of residues.The Biochemical journal · 2023Article
- Protein Phosphatase 2A with B' specificity subunits regulates the Hippo-Yorkie signaling axis in the Drosophila eye disc.Journal of cell science · 2022Article
- Kinetic Regulation of the Mammalian Sterile 20-like Kinase 2 (MST2).Biochemistry · 2022Article
- Regulation of MST complexes and activity via SARAH domain modifications.Biochemical Society transactions · 2021Review
- The regulatory networks of the Hippo signaling pathway in cancer development.Journal of Cancer · 2021Review
- Increasing kinase domain proximity promotes MST2 autophosphorylation during Hippo signaling.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Hippo pathway signaling limits cell growth and proliferation and maintains the stem-cell niche. These cellular events result from the coordinated activity of a core kinase cassette that is regulated, in part, by interactions involving Hippo, Salvador, and dRassF. These interactions are mediated by a conserved coiled-coil domain, termed SARAH, in each of these proteins. SARAH domain-mediated homodimerization of Hippo kinase leads to autophosphorylation and activation. Paradoxically, SARAH domain-mediated heterodimerization between Hippo and Salvador enhances Hippo kinase activity in cells, whereas complex formation with dRassF inhibits it. To better understand the mechanism by which each complex distinctly modulates Hippo kinase and pathway activity, here we biophysically characterized the entire suite of SARAH domain-mediated complexes. We purified the three SARAH domains from
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Registered trials
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