Evidence map›Paper›PMID 12642614›Full record

ArticleThe Journal of cell biology2003

Identification of an organelle-specific myosin V receptor.

Kuniko Ishikawa, Natalie L Catlett, Jennifer L Novak, Fusheng Tang, Johnathan J Nau, Lois S Weisman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

61 citing papers in PubMed, 120 citations in OpenAlex.

  1. Cell membrane asymmetries and cellular aging.The Biochemical journal · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. The signalling lipid PI3,5POpen biology · 2023
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021
    Review
  18. Article
  19. Article
  20. Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018
    Review

1 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

6 authors at 1 institution in 1 country.

Kuniko IshikawaDept. of Biochemistry, The University of Iowa, Iowa City, IA 52242, USA. lois-weisman@uiowa.edu
Natalie L Catlett
Jennifer L Novak
Fusheng Tang
Johnathan J Nau
Lois S Weisman
University of Iowa · US

Funding

Regulation of myosin V interaction with cargo-Equipment SupplementR01GM062261 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Lois S Weisman · 2001 to 2026
$5.8M
INTERDISCIPLINARY RESEARCH TRAINING PROGRAM ON AGINGT32AG000214 · NIA · UNIVERSITY OF IOWA · PI WALLACE, ROBERT BRUCE · 1991 to 2000
$164k
NIA NIH HHS T32 AG000214NIA NIH HHS T32 AG 00214NIGMS NIH HHS R01 GM062261NIGMS NIH HHS R01 GM62261
6 · The paper itself

Abstract

Class V myosins are widely distributed among diverse organisms and move cargo along actin filaments. Some myosin Vs move multiple types of cargo, where the timing of movement and the destinations of selected cargoes are unique. Here, we report the discovery of an organelle-specific myosin V receptor. Vac17p, a novel protein, is a component of the vacuole-specific receptor for Myo2p, a Saccharomyces cerevisiae myosin V. Vac17p interacts with the Myo2p cargo-binding domain, but not with vacuole inheritance-defective myo2 mutants that have single amino acid changes within this region. Moreover, a region of the Myo2p tail required specifically for secretory vesicle transport is neither required for vacuole inheritance nor for Vac17p-Myo2p interactions. Vac17p is localized on the vacuole membrane, and vacuole-associated Myo2p increases in proportion with an increase in Vac17p. Furthermore, Vac17p is not required for movement of other cargo moved by Myo2p. These findings demonstrate that Vac17p is a component of a vacuole-specific receptor for Myo2p. Organelle-specific receptors such as Vac17p provide a mechanism whereby a single type of myosin V can move diverse cargoes to distinct destinations at different times.

Indexed as

Vesicular Transport ProteinsActin CytoskeletonCells, CulturedGene Expression Regulation, FungalIntracellular MembranesMyosin Heavy ChainsMyosin Type VOrganellesProtein Structure, TertiaryProtein TransportReceptors, Cell SurfaceSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory VesiclesVacuolesMYO2 protein, S cerevisiaeMyosin Heavy ChainsMyosin Type VReceptors, Cell SurfaceSaccharomyces cerevisiae ProteinsVAC17 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID12642614
PMCPMC2173761
OpenAlexW2114268618

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.