Evidence map›Paper›PMID 22172676›Full record

ArticleDevelopmental cell2011

Myosin V transports secretory vesicles via a Rab GTPase cascade and interaction with the exocyst complex.

Yui Jin, Azmiri Sultana, Pallavi Gandhi, Edward Franklin, Susan Hamamoto, Amir R Khan, Mary Munson, Randy Schekman, Lois S Weisman

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

108 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
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  10. Roles for the canonical polarity machinery in thebioRxiv : the preprint server for biology · 2025
    Article
  11. Review
  12. Article
  13. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  14. The exocyst in context.Biochemical Society transactions · 2024
    Review
  15. Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

48 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

9 authors at 3 institutions in 2 countries.

Yui JinLife Sciences Institute, Department of Cell & Developmental Biology, University of Michigan, Ann Arbor, MI 48109-2216, USA.
Azmiri Sultana
Pallavi Gandhi
Edward Franklin
Susan Hamamoto
Amir R Khan
Mary Munson
Randy Schekman
Lois S Weisman
Trinity College Dublin · IEHoward Hughes Medical Institute · USUniversity of Michigan–Ann Arbor · US

Funding

Structure and Function of the Exocyst ComplexR01GM068803 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MUNSON, MARY · 2005 to 2021
$7.4M
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
Regulation of Myosin V Interaction with CargoR37GM062261 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WEISMAN, LOIS S · 2009 to 2018
$4.3M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM062261NIGMS NIH HHS R01 GM068803NIGMS NIH HHS R37 GM062261NIGMS NIH HHS R37 GM62261
6 · The paper itself

Abstract

Vesicle transport requires four steps: vesicle formation, movement, tethering, and fusion. In yeast, two Rab GTPases, Ypt31/32, are required for post-Golgi vesicle formation. A third Rab GTPase, Sec4, and the exocyst act in tethering and fusion of these vesicles. Vesicle production is coupled to transport via direct interaction between Ypt31/32 and the yeast myosin V, Myo2. Here we show that Myo2 interacts directly with Sec4 and the exocyst subunit Sec15. Disruption of these interactions results in compromised growth and the accumulation of secretory vesicles. We identified the Sec15-binding region on Myo2 and also identified residues on Sec15 required for interaction with Myo2. That Myo2 interacts with Sec15 uncovers additional roles for the exocyst as an adaptor for molecular motors and implies similar roles for structurally related tethering complexes. Moreover, these studies predict that for many pathways, molecular motors attach to vesicles prior to their formation and remain attached until fusion.

Indexed as

Amino Acid SubstitutionBinding SitesExocytosisMembrane FusionModels, MolecularMolecular Motor ProteinsMutagenesis, Site-DirectedMyosin Heavy ChainsMyosin Type VProtein Interaction Domains and Motifsrab GTP-Binding ProteinsRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory VesiclesSignal TransductionMolecular Motor ProteinsMYO2 protein, S cerevisiaeMyosin Heavy ChainsMyosin Type Vrab GTP-Binding ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSEC15 protein, S cerevisiaeSEC4 protein, S cerevisiaeVesicular Transport ProteinsYPT31 protein, S cerevisiaeYPT32 protein, S cerevisiae

Identifiers

PMID22172676
PMCPMC3241923
OpenAlexW1965688791

What OpenQuestion holds

Textmetadata
LicenceTDM
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.