Evidence map›Paper›PMID 11113201›Full record

ArticleMolecular and cellular biology2001

Wsc1 and Mid2 are cell surface sensors for cell wall integrity signaling that act through Rom2, a guanine nucleotide exchange factor for Rho1.

B Philip, D E Levin

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.

0numbers the graph read from it
0cells of the map it votes in
139citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

139 citing papers in PubMed, 305 citations in OpenAlex.

  1. Article
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  9. Transcriptional Reprogramming ofJournal of fungi (Basel, Switzerland) · 2023
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  15. Effect of Shock Waves on the Growth ofJournal of fungi (Basel, Switzerland) · 2022
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  20. Cell cycle arrest ofSTAR protocols · 2021
    Article

79 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

B PhilipDepartment of Biochemistry & Molecular Biology, School of Public Health, The Johns Hopkins University, Baltimore, Maryland 21205, USA. levin@welch.jhu.edu
D E Levin
Johns Hopkins University · US

Funding

ROLE OF PROTEIN KINASE C IN YEAST GROWTH CONTROLR01GM048533 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI LEVIN, DAVID E. · 1992 to 2025
$7.8M
NIGMS NIH HHS GM48533NIGMS NIH HHS R01 GM048533
6 · The paper itself

Abstract

Wsc1 and Mid2 are highly O-glycosylated cell surface proteins that reside in the plasma membrane of Saccharomyces cerevisiae. They have been proposed to function as mechanosensors of cell wall stress induced by wall remodeling during vegetative growth and pheromone-induced morphogenesis. These proteins are required for activation of the cell wall integrity signaling pathway that consists of the small G-protein Rho1, protein kinase C (Pkc1), and a mitogen-activated protein kinase cascade. We show here by two-hybrid experiments that the C-terminal cytoplasmic domains of Wsc1 and Mid2 interact with Rom2, a guanine nucleotide exchange factor (GEF) for Rho1. At least with regard to Wsc1, this interaction is mediated by the Rom2 N-terminal domain. This domain is distinct from the Rho1-interacting domain, suggesting that the GEF can interact simultaneously with a sensor and with Rho1. We also demonstrate that extracts from wsc1 and mid2 mutants are deficient in the ability to catalyze GTP loading of Rho1 in vitro, providing evidence that the function of the sensor-Rom2 interaction is to stimulate nucleotide exchange toward this G-protein. In a related line of investigation, we identified the PMT2 gene in a genetic screen for mutations that confer an additive cell lysis defect with a wsc1 null allele. Pmt2 is a member of a six-protein family in yeast that catalyzes the first step in O mannosylation of target proteins. We demonstrate that Mid2 is not mannosylated in a pmt2 mutant and that this modification is important for signaling by Mid2.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceCalcium-Binding ProteinsCell WallEnzyme ActivationGuanine Nucleotide Exchange FactorsIntracellular Signaling Peptides and ProteinsMannosyltransferasesMembrane GlycoproteinsMembrane ProteinsMutationPheromonesProtein BindingProtein Serine-Threonine KinasesProtein Structure, Tertiaryrho GTP-Binding ProteinsCalcium-Binding ProteinsGuanine Nucleotide Exchange FactorsIntracellular Signaling Peptides and ProteinsMannosyltransferasesMembrane GlycoproteinsMembrane ProteinsMID2 protein, S cerevisiaePheromonesprotein O-mannosyltransferaseProtein Serine-Threonine KinasesRHO1 protein, S cerevisiaerho GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSLG1 protein, S cerevisiae

Identifiers

PMID11113201
PMCPMC88800
OpenAlexW2142161768

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.