Evidence map›Paper›PMID 23019326›Full record

ArticleThe Journal of biological chemistry2012

Membrane protein Rim21 plays a central role in sensing ambient pH in Saccharomyces cerevisiae.

Keisuke Obara, Hayashi Yamamoto, Akio Kihara

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

40 citing papers in PubMed, 69 citations in OpenAlex.

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  8. Molecular association ofFrontiers in cellular and infection microbiology · 2023
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  12. Review
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  14. Review
  15. Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  16. Article
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  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Keisuke ObaraFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 062-0812, Japan.
Hayashi Yamamoto
Akio Kihara
Hokkaido University · JPTokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

External alkalization activates the Rim101 pathway in Saccharomyces cerevisiae. In this pathway, three integral membrane proteins, Rim21, Dfg16, and Rim9, are considered to be the components of the pH sensor machinery. However, how these proteins are involved in pH sensing is totally unknown. In this work, we investigated the localization, physical interaction, and interrelationship of Rim21, Dfg16, and Rim9. These proteins were found to form a complex and to localize to the plasma membrane in a patchy and mutually dependent manner. Their cellular level was also mutually dependent. In particular, the Rim21 level was significantly decreased in dfg16Δ and rim9Δ cells. Upon external alkalization, the proteins were internalized and degraded. We also demonstrate that the transient degradation of Rim21 completely suppressed the Rim101 pathway but that the degradation of Dfg16 or Rim9 did not. This finding strongly suggests that Rim21 is the pH sensor protein and that Dfg16 and Rim9 play auxiliary functions through maintaining the level of Rim21 and assisting in its plasma membrane localization. Even without external alkalization, the Rim101 pathway was activated in a Rim21-dependent manner by either protonophore treatment or depletion of phosphatidylserine in the inner leaflet of the plasma membrane, both of which caused plasma membrane depolarization like the external alkalization. Therefore, plasma membrane depolarization seems to be one of the key signals for the pH sensor molecule Rim21.

Indexed as

Amino Acid MotifsCell MembraneF-Box ProteinsGene DeletionGlycosylationGreen Fluorescent ProteinsHydrogen-Ion ConcentrationLipid BilayersLipidsMembrane ProteinsPhosphorylationPlasmidsProtein Processing, Post-TranslationalReceptors, Cell SurfaceSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsF-Box ProteinsGreen Fluorescent ProteinsLipid BilayersLipidsMembrane ProteinsMET30 protein, S cerevisiaeReceptors, Cell SurfaceRim21 protein, S cerevisiaeRIM9 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase Complexes

Identifiers

PMID23019326
PMCPMC3493892
OpenAlexW1965391415

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.