Evidence map›Paper›PMID 9412475›Full record

ArticleThe Journal of cell biology1997

Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton.

G Vaduva, N C Martin, A K Hopper

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

36 citing papers in PubMed, 112 citations in OpenAlex.

  1. Imaging the Actin Cytoskeleton in Live Budding Yeast Cells.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  2. Article
  3. Live-Cell Imaging of Mitochondria and the Actin Cytoskeleton in Budding Yeast.Methods in molecular biology (Clifton, N.J.) · 2016
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Actin and endocytosis: mechanisms and phylogeny.Current opinion in cell biology · 2009
    Review
  13. Review
  14. Article
  15. Article
  16. The yeast actin cytoskeleton: from cellular function to biochemical mechanism.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  17. Article
  18. The BAR domain proteins: molding membranes in fission, fusion, and phagy.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  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.

G VaduvaDepartment of Biochemistry and Molecular Biology, The Milton S. Hershey Medical Center, The Pennsylvania State University, Hershey, Pennsylvania 17033, USA.
N C Martin
A K Hopper
University of Louisville · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yeast verprolin, encoded by VRP1, is implicated in cell growth, cytoskeletal organization, endocytosis and mitochondrial protein distribution and function. We show that verprolin is also required for bipolar bud-site selection. Previously we reported that additional actin suppresses the temperature-dependent growth defect caused by a mutation in VRP1. Here we show that additional actin suppresses all known defects caused by vrp1-1 and conclude that the defects relate to an abnormal cytoskeleton. Using the two-hybrid system, we show that verprolin binds actin. An actin-binding domain maps to the LKKAET hexapeptide located in the first 70 amino acids. A similar hexapeptide in other acting-binding proteins was previously shown to be necessary for actin-binding activity. The entire 70- amino acid motif is conserved in novel higher eukaryotic proteins that we predict to be actin-binding, and also in the actin-binding proteins, WASP and N-WASP. Verprolin-GFP in live cells has a cell cycle-dependent distribution similar to the actin cortical cytoskeleton. In fixed cells hemagglutinin-tagged Vrp1p often co-localizes with actin in cortical patches. However, disassembly of the actin cytoskeleton using Latrunculin-A does not alter verprolin's location, indicating that verprolin establishes and maintains its location independent of the actin cytoskeleton. Verprolin is a new member of the actin-binding protein family that serves as a polarity development protein, perhaps by anchoring actin. We speculate that the effects of verprolin upon the actin cytoskeleton might influence mitochondrial protein sorting/function via mRNA distribution.

Indexed as

Saccharomyces cerevisiae ProteinsActinsAllelesAmino Acid SequenceBinding SitesCell PolarityCytoskeletonEndocytosisFungal ProteinsMicrofilament ProteinsMitochondriaMolecular Sequence DataMorphogenesisNucleic Acid HybridizationPhenotypeSaccharomyces cerevisiaeActinsFungal ProteinsMicrofilament ProteinsSaccharomyces cerevisiae ProteinsVRP1 protein, S cerevisiae

Identifiers

PMID9412475
PMCPMC2132640
OpenAlexW2004479585

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.