Evidence map›Paper›PMID 19767735›Full record

ArticleNature chemical biology2009

The yeast Wsc1 cell surface sensor behaves like a nanospring in vivo.

Vincent Dupres, David Alsteens, Sabrina Wilk, Benjamin Hansen, Jürgen J Heinisch, Yves F Dufrêne

Abstract read
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In one paragraph

Article in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

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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

6 authors.

Vincent DupresUnité de Chimie des Interfaces, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
David Alsteens
Sabrina Wilk
Benjamin Hansen
Jürgen J Heinisch
Yves F Dufrêne

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here we report on in vivo measurement of the mechanical behavior of a cell surface sensor using single-molecule atomic force microscopy. We focus on the yeast wall stress component sensor Wsc1, a plasma membrane protein that is thought to function as a rigid probe of the cell wall status. We first map the distribution of individual histidine-tagged sensors on living yeast cells by scanning the cell surface with atomic force microscopy tips carrying nitrilotriacetate groups. We then show that Wsc1 behaves like a linear nanospring that is capable of resisting high mechanical force and of responding to cell surface stress. Both a genomic pmt4 deletion and the insertion of a stretch of glycines in Wsc1 result in substantial alterations in protein spring properties, supporting the important role of glycosylation at the extracellular serine/threonine-rich region.

Indexed as

Biosensing TechniquesCell MembraneCells, ImmobilizedCell WallIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMembrane ProteinsMicroscopy, Atomic ForceModels, MolecularProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolutionsStress, MechanicalIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMembrane ProteinsMID2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSLG1 protein, S cerevisiaeSolutions

Identifiers

PMID19767735

What OpenQuestion holds

Textmetadata
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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.