Evidence map›Paper›PMID 8682864›Full record

ArticleThe Journal of cell biology1996

Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton.

H V Goodson, B L Anderson, H M Warrick, L A Pon, J A Spudich

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
16.3field-weighted citation impact, top 1% 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

95 citing papers in PubMed, 230 citations in OpenAlex.

  1. The Role of Arp2/3 in End-Resection During DNA Double-Strand Break Repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
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  8. Article
  9. Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023
    Article
  10. Self-organizing actin networks drive sequential endocytic protein recruitment and vesicle release on synthetic lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Yeast as a Model to Find New Drugs and Drug Targets forInternational journal of molecular sciences · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

35 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

5 authors at 1 institution in 1 country.

H V GoodsonDepartment of Biochemistry, Stanford University, CA 94305, USA.
B L Anderson
H M Warrick
L A Pon
J A Spudich
Stanford University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007367 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI REINER, STEVEN L · 1985 to 2021
$25.1M
MITOCHONDRIAL MOTILITY AND INHERITANCER01GM045735 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PON, LIZA A · 1993 to 2016
$4.2M
HOMOLOGOUS RECOMBINATION IN DICTYOSTELIUMR01GM040509 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES A · 1988 to 2001
$416k
NIGMS NIH HHS 5T32 GM07367NIGMS NIH HHS GM40509NIGMS NIH HHS GM45735
6 · The paper itself

Abstract

The organization of the actin cytoskeleton plays a critical role in cell physiology in motile and nonmotile organisms. Nonetheless, the function of the actin based motor molecules, members of the myosin superfamily, is not well understood. Deletion of MYO3, a yeast gene encoding a "classic" myosin I, has no detectable phenotype. We used a synthetic lethality screen to uncover genes whose functions might overlap with those of MYO3 and identified a second yeast myosin 1 gene, MYO5. MYO5 shows 86 and 62% identity to MYO3 across the motor and non-motor regions. Both genes contain an amino terminal motor domain, a neck region containing two IQ motifs, and a tail domain consisting of a positively charged region, a proline-rich region containing sequences implicated in ATP-insensitive actin binding, and an SH3 domain. Although myo5 deletion mutants have no detectable phenotype, yeast strains deleted for both MYO3 and MYO5 have severe defects in growth and actin cytoskeletal organization. Double deletion mutants also display phenotypes associated with actin disorganization including accumulation of intracellular membranes and vesicles, cell rounding, random bud site selection, sensitivity to high osmotic strength, and low pH as well as defects in chitin and cell wall deposition, invertase secretion, and fluid phase endocytosis. Indirect immunofluorescence studies using epitope-tagged Myo5p indicate that Myo5p is localized at actin patches. These results indicate that MYO3 and MYO5 encode classical myosin I proteins with overlapping functions and suggest a role for Myo3p and Myo5p in organization of the actin cytoskeleton of Saccharomyces cerevisiae.

Indexed as

Myosin Type ISaccharomyces cerevisiae ProteinsActinsAmino Acid SequenceBase Sequencebeta-FructofuranosidaseCell MembraneChitinCloning, MolecularCytoskeletonDNA, FungalEndocytosisFungal ProteinsGenes, FungalGenes, LethalGenetic Complementation TestActinsbeta-FructofuranosidaseChitinDNA, FungalFungal ProteinsGlycoside HydrolasesMYO5 protein, S cerevisiaeMyosinsMyosin Type ISaccharomyces cerevisiae Proteins

Identifiers

PMID8682864
PMCPMC2120899
OpenAlexW2093082265

What OpenQuestion holds

Textmetadata
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.