ArticleScientific reports2019
New type of interaction between the SARAH domain of the tumour suppressor RASSF1A and its mitotic kinase Aurora A.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 4 citations in OpenAlex.
- 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
- Biophysical characterization of SARAH domain-mediated multimerization of Hippo pathway complexes inThe Journal of biological chemistry · 2020Article
- A versatile modular vector set for optimizing protein expression among bacterial, yeast, insect and mammalian hosts.PloS one · 2019Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tumour suppressor protein RASSF1A is phosphorylated by Aurora A kinase, thereby impairing its tumour suppressor function. Consequently, inhibiting the interaction between Aurora A and RASSF1A may be used for anti-tumour therapy. We used recombinant variants of RASSF1A to map the sites of interaction with Aurora A. The phosphorylation kinetics of three truncated RASSF1A variants has been analysed. Compared to the RASSF1A form lacking the 120 residue long N-terminal part, the K
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