Evidence map›Paper›PMID 10562281›Full record

ArticleThe Journal of cell biology1999

The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting.

D Schott, J Ho, D Pruyne, A Bretscher

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

121 citing papers in PubMed, 252 citations in OpenAlex.

  1. Article
  2. Endocytosis and trans-Golgi Network in Yeast.Sub-cellular biochemistry · 2026
    Review
  3. Article
  4. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021
    Review
  13. Article
  14. Journal of cell science · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. The tail domain of theJournal of cell science · 2018
    Article
  19. MYO18A: An unusual myosin.Advances in biological regulation · 2018
    Review
  20. Article

61 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

4 authors at 1 institution in 1 country.

D SchottDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.
J Ho
D Pruyne
A Bretscher
Cornell University · US

Funding

MICROFILAMENTS IN THE YEAST SACCHAROMYCES CEREVISIAER01GM039066 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BRETSCHER, ANTHONY P. · 1988 to 2018
$7.3M
NIGMS NIH HHS GM39066NIGMS NIH HHS R01 GM039066
6 · The paper itself

Abstract

MYO2 encodes a type V myosin heavy chain needed for the targeting of vacuoles and secretory vesicles to the growing bud of yeast. Here we describe new myo2 alleles containing conditional lethal mutations in the COOH-terminal tail domain. Within 5 min of shifting to the restrictive temperature, the polarized distribution of secretory vesicles is abolished without affecting the distribution of actin or the mutant Myo2p, showing that the tail has a direct role in vesicle targeting. We also show that the actin cable-dependent translocation of Myo2p to growth sites does not require secretory vesicle cargo. Although a fusion protein containing the Myo2p tail also concentrates at growth sites, this accumulation depends on the polarized delivery of secretory vesicles, implying that the Myo2p tail binds to secretory vesicles. Most of the new mutations alter a region of the Myo2p tail conserved with vertebrate myosin Vs but divergent from Myo4p, the myosin V involved in mRNA transport, and genetic data suggest that the tail interacts with Smy1p, a kinesin homologue, and Sec4p, a vesicle-associated Rab protein. The data support a model in which the Myo2p tail tethers secretory vesicles, and the motor transports them down polarized actin cables to the site of exocytosis.

Indexed as

Myosin Heavy ChainsMyosin Type IIMyosin Type VSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsAllelesAmino Acid SequenceAmino Acid SubstitutionAnimalsCell PolarityConsensus SequenceCytoplasmic GranulesDictyosteliumEvolution, MolecularFungal ProteinsGenotypeFungal ProteinsMYO2 protein, S cerevisiaeMYO2 protein, S pombeMyosin Heavy ChainsMyosinsMyosin Type IIMyosin Type VRecombinant ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID10562281
PMCPMC2156159
OpenAlexW1976264442

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.