Evidence map›Paper›PMID 20005107›Full record

ArticleCurrent biology : CB2009

A nonprocessive class V myosin drives cargo processively when a kinesin- related protein is a passenger.

Alex R Hodges, Carol S Bookwalter, Elena B Krementsova, Kathleen M Trybus

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

38 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Molecular features of Myosin F adapted for driving actin flows inbioRxiv : the preprint server for biology · 2025
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  16. Vascular disease-causing mutation R258C in ACTA2 disrupts actin dynamics and interaction with myosin.Proceedings of the National Academy of Sciences of the United States of America · 2015
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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.

Alex R HodgesDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA.
Carol S Bookwalter
Elena B Krementsova
Kathleen M Trybus
University of Vermont · US

Funding

Proteomics Core for Neuroscience P20 RR16435P20RR016435 · NCRR · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI SPEES, JEFFREY L · 2001 to 2010
$23.5M
MUTATIONAL STUDIES OF PROCESSIVE MYOSIN MOTORSR01GM078097 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 2007 to 2019
$4.8M
NCRR NIH HHS 2 P20 RR016435-06NCRR NIH HHS P20 RR016435NIGMS NIH HHS GM078097NIGMS NIH HHS R01 GM078097
6 · The paper itself

Abstract

During secretory events, kinesin transports cargo along microtubules and then shifts control to myosin V for delivery on actin filaments to the cell membrane [1]. When kinesin and myosin V are present on the same cargo, kinesin interacts electrostatically with actin to enhance myosin V-based transport in vitro [2]. The relevance of this observation within the cell was questioned. In budding yeast, overexpression of a kinesin-family protein (Smy1p) suppressed a transport defect in a strain with a mutant class V myosin (Myo2p) [3]. We postulate that this is a cellular manifestation of the in vitro observation. We demonstrate that Smy1p binds electrostatically to actin bundles. Although a single Myo2p cannot transport cargo along actin bundles, addition of Smy1p causes the complex to undergo long-range, continuous movement. We propose that the kinesin-family protein acts as a tether that prevents cargo dissociation from actin, allowing the myosin to take many steps before dissociating. We demonstrate that both the tether and the motor reside on moving secretory vesicles in yeast cells, a necessary feature for this mechanism to apply in vivo. The presence of both kinesin and myosin on the same cargo may be a general mechanism to enhance cellular transport in yeast and higher organisms.

Indexed as

ActinsBinding, CompetitiveBiological TransportCarrier ProteinsElectrophoresis, Polyacrylamide GelMicroscopy, FluorescenceMicrotubule-Associated ProteinsModels, MolecularMyosin Heavy ChainsMyosin Type VQuantum DotsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsCarrier Proteinskinesin-like protein 1Microtubule-Associated ProteinsMYO2 protein, S cerevisiaeMyosin Heavy ChainsMyosin Type VSaccharomyces cerevisiae Proteins

Identifiers

PMID20005107
PMCPMC2904613
OpenAlexW1990179178

What OpenQuestion holds

Textmetadata
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.