ArticleNature communications2015
Osmosensing and scaffolding functions of the oligomeric four-transmembrane domain osmosensor Sho1.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 57 citations in OpenAlex.
- Rice Lectin Protein r40c1 Interacts With Magnaporthe oryzae Sho1 Protein to Regulate Leaf Blast Resistance.Plant, cell & environment · 2026Article
- Article
- Hybrid histidine kinases shape the architecture of the high osmolarity glycerol (HOG) pathway: from Saccharomyces cerevisiae to the priority pathogen Aspergillus fumigatus and other filamentous fungi.FEMS microbiology reviews · 2026Review
- Engineered Microbial Strains for Co-fermentation of C5 and C6 Sugars to Produce Cellulosic Ethanol.Advances in biochemical engineering/biotechnology · 2026Review
- The Arabidopsis PM19L1 Protein Functions as a Regulator of Germination Under Osmotic Stress.Plant direct · 2025Article
- Unremodeled GPI-anchored proteins at the plasma membrane trigger aberrant endocytosis.Life science alliance · 2025Article
- Conserved signaling modules regulate filamentous growth in fungi: a model for eukaryotic cell differentiation.Genetics · 2024Review
- Shared and redundant proteins coordinate signal cross-talk between MAPK pathways in yeast.Molecular biology of the cell · 2024Article
- A cryptic promoter in the exon of HKR1 drives expression of a truncated form of Hkr1 in Saccharomyces cerevisiae.PloS one · 2024Article
- Yeast osmoregulation - glycerol still in pole position.FEMS yeast research · 2022Review
- Sensing and Responding to Hypersaline Conditions and the HOG Signal Transduction Pathway in Fungi Isolated from Hypersaline Environments:Journal of fungi (Basel, Switzerland) · 2021Review
- Cdc42-Specific GTPase-Activating Protein Rga1 Squelches Crosstalk between the High-Osmolarity Glycerol (HOG) and Mating Pheromone Response MAPK Pathways.Biomolecules · 2021Article
- Recruitment of Xrn1 to stress-induced genes allows efficient transcription by controlling RNA polymerase II backtracking.RNA biology · 2021Article
- Building predictive signaling models by perturbing yeast cells with time-varying stimulations resulting in distinct signaling responses.STAR protocols · 2021Article
- Spatiotemporal control of pathway sensors and cross-pathway feedback regulate a differentiation MAPK pathway in yeast.Journal of cell science · 2021Article
- Shaker-IR K+ channel gating in heavy water: Role of structural water molecules in inactivation.The Journal of general physiology · 2021Article
- Article
- The High Osmolarity Glycerol (HOG) Pathway Functions in Osmosensing, Trap Morphogenesis and Conidiation of the Nematode-Trapping FungusJournal of fungi (Basel, Switzerland) · 2020Article
- The transmembrane protein MaSho1 negatively regulates conidial yield by shifting the conidiation pattern in Metarhizium acridum.Applied microbiology and biotechnology · 2020Article
- Functions for Cdc42p BEM adaptors in regulating a differentiation-type MAP kinase pathway.Molecular biology of the cell · 2020Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast high osmolarity glycerol (HOG) pathway activates the Hog1 MAP kinase, which coordinates adaptation to high osmolarity conditions. Here we demonstrate that the four-transmembrane (TM) domain protein Sho1 is an osmosensor in the HKR1 sub-branch of the HOG pathway. Crosslinking studies indicate that Sho1 forms planar oligomers of the dimers-of-trimers architecture by dimerizing at the TM1/TM4 interface and trimerizing at the TM2/TM3 interface. High external osmolarity induces structural changes in the Sho1 TM domains and Sho1 binding to the cytoplasmic adaptor protein Ste50, which leads to Hog1 activation. Besides its osmosensing function, the Sho1 oligomer serves as a scaffold. By binding to the TM proteins Opy2 and Hkr1 at the TM1/TM4 and TM2/TM3 interface, respectively, Sho1 forms a multi-component signalling complex that is essential for Hog1 activation. Our results illuminate how the four TM domains of Sho1 dictate the oligomer structure as well as its osmosensing and scaffolding functions.
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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.