ArticleCommunicative & integrative biology2013
Phosphorelay-dependent and -independent regulation of MAPKKK by the Mcs4 response regulator in fission yeast.
Article in Communicative & integrative biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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
5 citing papers in PubMed.
- A Redox-Sensitive Thiol in Wis1 Modulates the Fission Yeast Mitogen-Activated Protein Kinase Response to HMolecular and cellular biology · 2020Article
- The yeasts phosphorelay systems: a comparative view.World journal of microbiology & biotechnology · 2017Review
- Stress sensitivity of a fission yeast strain lacking histidine kinases is rescued by the ectopic expression of Chk1 from Candida albicans.Current genetics · 2017Article
- A Perspective on CRN Proteins in the Genomics Age: Evolution, Classification, Delivery and Function Revisited.Frontiers in plant science · 2017Review
- Transposons to toxins: the provenance, architecture and diversification of a widespread class of eukaryotic effectors.Nucleic acids research · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
In a "two-component system," extracellular stimuli are transmitted by the transfer of a phosphoryl group from a sensor histidine kinase to a response regulator (RR), a mechanism referred to as phosphorelay. In the fission yeast Schizosaccharomyces pombe, peroxide stress signals are transmitted by phosphorelay to the Mcs4 RR, which activates the Spc1 MAP kinase (MAPK) cascade. We previously demonstrated that a glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) physically interacts with Mcs4 and promotes phosphorelay signaling to Mcs4. Independently of the phosphorelay mechanism, Mcs4 also plays a critical role in osmostress signaling, as a part of the stable ternary complex with the Wis4 and Win1 MAPK kinase kinases (MAPKKKs). Interestingly, GAPDH dissociates from Mcs4 upon osmostress, while oxidative stress promotes their association. The Mcs4 RR may serve as a switching hub that mediates activation of the Wis4-Win1 MAPKKK heteromer in response to different forms of stress.
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Registered trials
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