Evidence map›Paper›PMID 17065552›Full record

ArticleMolecular biology of the cell2007

NPFXD-mediated endocytosis is required for polarity and function of a yeast cell wall stress sensor.

Hai Lan Piao, Iara M P Machado, Gregory S Payne

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

45 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
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  11. Integrins in disguise - mechanosensors inMicrobial cell (Graz, Austria) · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Protein kinase C and calcineurin cooperatively mediate cell survival under compressive mechanical stress.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Article
  20. Article
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 1 institution in 1 country.

Hai Lan PiaoDepartment of Biological Chemistry, David Geffen School of Medicine, University of California-Los Angeles, Los Angeles, CA 90095, USA.
Iara M P Machado
Gregory S Payne
University of California, Los Angeles · US

Funding

MOLECULAR STUDIES OF SELECTIVE PROTEIN TRANSPORTR01GM039040 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI PAYNE, GREGORY S · 1988 to 2016
$6.4M
NIGMS NIH HHS GM39040NIGMS NIH HHS R01 GM039040
6 · The paper itself

Abstract

The actin-associated protein Sla1p, through its SHD1 domain, acts as an adaptor for the NPFX(1,2)D endocytic targeting signal in yeast. Here we report that Wsc1p, a cell wall stress sensor, depends on this signal-adaptor pair for endocytosis. Mutation of NPFDD in Wsc1p or expression of Sla1p lacking SHD1 blocked Wsc1p internalization. By live cell imaging, endocytically defective Wsc1p was not concentrated at sites of endocytosis. Polarized distribution of Wsc1p to regions of cell growth was lost in the absence of endocytosis. Mutations in genes necessary for endosome to Golgi traffic caused redistribution of Wsc1p from the cell surface to internal compartments, indicative of recycling. Inhibition of Wsc1p endocytosis caused defects in polarized deposition of the cell wall and increased sensitivity to perturbation of cell wall synthesis. Our results reveal that the NPFX(1,2)D-Sla1p system is responsible for directing Wsc1p into an endocytosis and recycling pathway necessary to maintain yeast cell wall polarity. The dynamic localization of Wsc1p, a sensor of the extracellular wall in yeast, resembles polarized distribution of certain extracellular matrix-sensing integrins through endocytic recycling.

Indexed as

Cell PolarityEndocytosisSignal TransductionAmino Acid MotifsCarrier ProteinsCell MembraneCell WallCytoskeletal ProteinsMembrane ProteinsPeptide FragmentsProtein BindingProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarrier ProteinsCytoskeletal ProteinsMembrane ProteinsPeptide FragmentsSaccharomyces cerevisiae ProteinsSLA1 protein, S cerevisiaeSLG1 protein, S cerevisiae

Identifiers

PMID17065552
PMCPMC1751320
OpenAlexW2137031771

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.