ArticlePLoS computational biology2016
SARAH Domain-Mediated MST2-RASSF Dimeric Interactions.
Article in PLoS computational biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed.
- The Dual Role ofBiology · 2025Review
- MST2 methylation by PRMT5 inhibits Hippo signaling and promotes pancreatic cancer progression.The EMBO journal · 2023Article
- Apoptosis in Type 2 Diabetes: Can It Be Prevented? Hippo Pathway Prospects.International journal of molecular sciences · 2022Review
- Regulation of MST complexes and activity via SARAH domain modifications.Biochemical Society transactions · 2021Review
- Mob Family Proteins: Regulatory Partners in Hippo and Hippo-Like Intracellular Signaling Pathways.Frontiers in cell and developmental biology · 2020Review
- New type of interaction between the SARAH domain of the tumour suppressor RASSF1A and its mitotic kinase Aurora A.Scientific reports · 2019Article
- Amyloid Fibril Design: Limiting Structural Polymorphism in Alzheimer's Aβ Protofilaments.The journal of physical chemistry. B · 2018Article
- Autoinhibition in Ras effectors Raf, PI3Kα, and RASSF5: a comprehensive review underscoring the challenges in pharmacological intervention.Biophysical reviews · 2018Review
- Ubiquitin-Dependent Regulation of the Mammalian Hippo Pathway: Therapeutic Implications for Cancer.Cancers · 2018Review
- Oncogenic Ras Isoforms Signaling Specificity at the Membrane.Cancer research · 2018Review
- The dynamic mechanism of RASSF5 and MST kinase activation by Ras.Physical chemistry chemical physics : PCCP · 2017Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RASSF enzymes act as key apoptosis activators and tumor suppressors, being downregulated in many human cancers, although their exact regulatory roles remain unknown. A key downstream event in the RASSF pathway is the regulation of MST kinases, which are main effectors of RASSF-induced apoptosis. The regulation of MST1/2 includes both homo- and heterodimerization, mediated by helical SARAH domains, though the underlying molecular interaction mechanism is unclear. Here, we study the interactions between RASSF1A, RASSF5, and MST2 SARAH domains by using both atomistic molecular simulation techniques and experiments. We construct and study models of MST2 homodimers and MST2-RASSF SARAH heterodimers, and we identify the factors that control their high molecular stability. In addition, we also analyze both computationally and experimentally the interactions of MST2 SARAH domains with a series of synthetic peptides particularly designed to bind to it, and hope that our approach can be used to address some of the challenging problems in designing new anti-cancer drugs.
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Registered trials
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