Evidence map›Paper›PMID 20164185›Full record

ArticleThe Journal of biological chemistry2010

Interactions among HAMP domain repeats act as an osmosensing molecular switch in group III hybrid histidine kinases from fungi.

Netrapal Meena, Harsimran Kaur, Alok K Mondal

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.6field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 70 citations in OpenAlex.

  1. Conformational diversity in poly-HAMP arrays and its implications for signal transduction.Protein science : a publication of the Protein Society · 2026
    Article
  2. Review
  3. Article
  4. Journal of fungi (Basel, Switzerland) · 2022
    Article
  5. Review
  6. Article
  7. Osmosensing by WNK Kinases.Molecular biology of the cell · 2021
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Network of nutrient-sensing pathways and a conserved kinase cascade integrate osmolarity and carbon sensing inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Are Aquaporins the Missing Transmembrane Osmosensors?The Journal of membrane biology · 2015
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Netrapal MeenaInstitute of Microbial Technology, Council of Scientific and Industrial Research, Chandigarh, India.
Harsimran Kaur
Alok K Mondal
Council of Scientific and Industrial Research · INInstitute of Microbial Technology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The members of group III hybrid histidine kinases (HHK) are ubiquitous in fungi. Group III HHK have been implicated to function as osmosensors in the high osmolarity glycerol (HOG) pathway that is essential for fungal survival under high osmolarity stress. Recent literature suggests that group III HHK are also involved in conidia formation, virulence in several filamentous fungi, and are an excellent molecular target for antifungal agents. Thus, group III HHK constitute a very important group of sensor kinases. Structurally, group III HHK are distinct from Sln1p, the osmosensing HHK that regulates the HOG pathway in Saccharomyces cerevisiae. Group III HHK lack any transmembrane domain and typically contain HAMP domain repeats at the N terminus. Until now, it is not clear how group III HHK function as an osmosensor to regulate the HOG pathway. To investigate this, we undertook molecular characterization of DhNIK1, an ortholog from osmotolerant yeast Debaryomyces hansenii. We show here that DhNIK1 could complement sln1 mutation in S. cerevisiae thereby confirming its role as a bona fide osmosensor. We further investigated the role of HAMP domains by deleting them systematically. Our results clearly indicate that the HAMP4 domain is crucial for osmosensing by DhNik1p. Most importantly, we also show that the alternative interaction among the HAMP domains regulates the activity of DhNik1p like an "on-off switch" and thus provides, for the first time, an insight into the molecular mechanism of osmosensing by this group of HHKs.

Indexed as

Amino Acid SequenceDebaryomycesFungiGenes, FungalGenetic Complementation TestHistidine KinaseModels, MolecularMolecular Sequence DataMutationOsmolar ConcentrationPhylogenyProtein KinasesProtein Structure, TertiaryRecombinant ProteinsRepetitive Sequences, Amino AcidSaccharomyces cerevisiaeHistidine KinaseProtein KinasesRecombinant Proteins

Identifiers

PMID20164185
PMCPMC2852951
OpenAlexW2012241820

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.