Evidence map›Paper›PMID 25660542›Full record

ArticleCurrent biology : CB2015

Control of the initiation and termination of kinesin-1-driven transport by myosin-Ic and nonmuscle tropomyosin.

Betsy B McIntosh, Erika L F Holzbaur, E Michael Ostap

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Cholesterol in the cargo membrane amplifies tau inhibition of kinesin-1-based transport.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Review
  6. Microtubules in insulin action: what's on the tube?Trends in endocrinology and metabolism: TEM · 2021
    Review
  7. Review
  8. Review
  9. Variant R94C inJournal of the American Heart Association · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Myosin-I molecular motors at a glance.Journal of cell science · 2016
    Review
  17. Article
  18. Article
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

3 authors at 1 institution in 1 country.

Betsy B McIntoshThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6085, USA.
Erika L F HolzbaurThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6085, USA. Electronic address: holzbaur@mail.med.upenn.edu.
E Michael OstapThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6085, USA. Electronic address: ostap@mail.med.upenn.edu.
University of Pennsylvania · US

Funding

Role of Myosin-l in Membrane Dynamics and TransportP01GM087253 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOLZBAUR, ERIKA L · 2009 to 2018
$15.3M
Training in Muscle Biology and Muscle DiseaseT32AR053461 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2006 to 2025
$4.9M
NIAMS NIH HHS T32 AR053461NIAMS NIH HHS T32 AR053461-08NIGMS NIH HHS P01 GM087253NIGMS NIH HHS P01 GM087253-10
6 · The paper itself

Abstract

Intracellular transport is largely driven by processive microtubule- and actin-based molecular motors. Nonprocessive motors have also been localized to trafficking cargos, but their roles are not well understood. Myosin-Ic (Myo1c), a nonprocessive actin motor, functions in a variety of exocytic events, although the underlying mechanisms are not yet clear. To investigate the interplay between myosin-I and the canonical long-distance transport motor kinesin-1, we attached both motor types to lipid membrane-coated bead cargo, using an attachment strategy that allows motors to actively reorganize within the membrane in response to the local cytoskeletal environment. We compared the motility of kinesin-1-driven cargos in the absence and presence of Myo1c at engineered actin/microtubule intersections. We found that Myo1c significantly increases the frequency of kinesin-1-driven microtubule-based runs that begin at actin/microtubule intersections. Myo1c also regulates the termination of processive runs. Beads with both motors bound have a significantly higher probability of pausing at actin/microtubule intersections, remaining tethered for an average of 20 s, with some pauses lasting longer than 200 s. The actin-binding protein nonmuscle tropomyosin (Tm) provides spatially specific regulation of interactions between myosin motors and actin filaments in vivo; in the crossed-filament in vitro assay, we found that Tm2-actin abolishes Myo1c-specific effects on both run initiation and run termination. Together, these observations suggest Myo1c is important for the selective initiation and termination of kinesin-1-driven runs along microtubules at specific actin filament populations within the cell.

Indexed as

Cell MovementCytoskeletonHumansKinesinsMyosin Type IProtein TransportTropomyosinKIF5B protein, humanKinesinsMYO1C protein, humanMyosin Type ITPM2 protein, humanTropomyosin

Identifiers

PMID25660542
PMCPMC4334669
OpenAlexW2051334453

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.