Evidence map›Paper›PMID 33184698›Full record

ReviewCurrent genetics2021

The Rim101 pathway mediates adaptation to external alkalization and altered lipid asymmetry: hypothesis describing the detection of distinct stresses by the Rim21 sensor protein.

Keisuke Obara, Takumi Kamura

Erratum issuedAbstract readReview
PubMed Publisher
In one paragraph

Review in Current genetics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Ppn2 Polyphosphatase Improves the Ability ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  2. Article
  3. Article
  4. Review
  5. Journal of fungi (Basel, Switzerland) · 2022
    Article
  6. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Keisuke ObaraDivision of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan. obara.keisuke@g.mbox.nagoya-u.ac.jp.ORCID http://orcid.org/0000-0002-2441-0907
Takumi KamuraDivision of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan. z47617a@nucc.cc.nagoya-u.ac.jp.

Funding

Japan Society for the Promotion of Science 19K06561
6 · The paper itself

Abstract

Yeast cells adapt to alkaline conditions by activating the Rim101 alkali-responsive pathway. Rim21 acts as a sensor in the Rim101 pathway and detects extracellular alkalization. Interestingly, Rim21 is also known to be activated by alterations involving the lipid asymmetry of the plasma membrane. In this study, we briefly summarize the mechanism of activation and the signal transduction cascade of the Rim101 pathway and propose a hypothesis on how Rim21 is able to detect distinct signals, particularly external alkalization, and altered lipid asymmetry. We found that external alkalization can suppress transbilayer movements of phospholipids between the two leaflets of the plasma membrane, which may lead to the disturbance of the lipid asymmetry of the plasma membrane. Therefore, we propose that external alteration is at least partly sensed by Rim21 through alterations in lipid asymmetry. Understanding this activation mechanism could greatly contribute to drug development against fungal infections.

Indexed as

Adaptation, PhysiologicalCell MembraneLipidsReceptors, Cell SurfaceRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionLipidsReceptors, Cell SurfaceRepressor ProteinsRIM101 protein, S cerevisiaeRim21 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsAlkaliLipid asymmetryPlasma membraneRim101 pathwayStress responseYeast

Identifiers

What OpenQuestion holds

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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.