Evidence map›Paper›PMID 10512884›Full record

ArticleMolecular biology of the cell1999

The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex.

A Madania, P Dumoulin, S Grava, H Kitamoto, C Schärer-Brodbeck, A Soulard, V Moreau, B Winsor

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

77 citing papers in PubMed, 163 citations in OpenAlex.

  1. Article
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  6. Regulation of membrane scission in yeast endocytosis.Molecular biology of the cell · 2022
    Article
  7. Imaging the Actin Cytoskeleton in Live Budding Yeast Cells.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Article
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  13. Article
  14. Prions, Chaperones, and Proteostasis in Yeast.Cold Spring Harbor perspectives in biology · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Live-Cell Imaging of Mitochondria and the Actin Cytoskeleton in Budding Yeast.Methods in molecular biology (Clifton, N.J.) · 2016
    Article
  19. Article
  20. Membrane trafficking in the yeast Saccharomyces cerevisiae model.International journal of molecular sciences · 2015
    Review

17 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

8 authors at 2 institutions in 2 countries.

A MadaniaMécanismes Moléculaires de la Division Cellulaire et du Développement, Unité Propre de Recherche 9005 du Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, F-67084 Strasbourg, France.
P Dumoulin
S Grava
H Kitamoto
C Schärer-Brodbeck
A Soulard
V Moreau
B Winsor
Institut de Biologie Moléculaire et Cellulaire · FRUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yeast Las17 protein is homologous to the Wiskott-Aldrich Syndrome protein, which is implicated in severe immunodeficiency. Las17p/Bee1p has been shown to be important for actin patch assembly and actin polymerization. Here we show that Las17p interacts with the Arp2/3 complex. LAS17 is an allele-specific multicopy suppressor of ARP2 and ARP3 mutations; overexpression restores both actin patch organization and endocytosis defects in ARP2 temperature-sensitive (ts) cells. Six of seven ARP2 ts mutants and at least one ARP3 ts mutant are synthetically lethal with las17Delta ts confirming functional interaction with the Arp2/3 complex. Further characterization of las17Delta cells showed that receptor-mediated internalization of alpha factor by the Ste2 receptor is severely defective. The polarity of normal bipolar bud site selection is lost. Las17-gfp remains localized in cortical patches in vivo independently of polymerized actin and is required for the polarized localization of Arp2/3 as well as actin. Coimmunoprecipitation of Arp2p with Las17p indicates that Las17p interacts directly with the complex. Two hybrid results also suggest that Las17p interacts with actin, verprolin, Rvs167p and several other proteins including Src homology 3 (SH3) domain proteins, suggesting that Las17p may integrate signals from different regulatory cascades destined for the Arp2/3p complex and the actin cytoskeleton.

Indexed as

Cytoskeletal ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsActin-Related Protein 2Actin-Related Protein 3ActinsEndocytosisFungal ProteinsGene Expression Regulation, FungalGreen Fluorescent ProteinsHumansLuminescent ProteinsMating FactorMicroscopy, FluorescenceMutationPeptidesActin-Related Protein 2Actin-Related Protein 3ActinsACTR2 protein, humanACTR3 protein, humanCytoskeletal ProteinsFungal ProteinsGreen Fluorescent ProteinsLAS17 protein, S cerevisiaeLuminescent ProteinsMating FactorPeptidesReceptors, Mating FactorReceptors, PeptideRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsWiskott-Aldrich Syndrome Protein

Identifiers

PMID10512884
PMCPMC25621
OpenAlexW2099769257

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.