Evidence map›Paper›PMID 29337076›Full record

ArticleCurrent biology : CB2018

Opposing Kinesin and Myosin-I Motors Drive Membrane Deformation and Tubulation along Engineered Cytoskeletal Networks.

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

Abstract read
In one paragraph

Article in Current biology : CB, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

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  13. Intracellular cargo transport by single-headed kinesin motors.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Review
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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.

Betsy B McIntoshThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6085, USA; Center for Engineering MechanoBiology, University of Pennsylvania, Philadelphia, PA 19104-6085, USA.
Serapion PyrpassopoulosThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6085, USA; Center for Engineering MechanoBiology, 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; Center for Engineering MechanoBiology, University of Pennsylvania, Philadelphia, PA 19104-6085, USA. Electronic address: holzbaur@pennmedicine.upenn.edu.
E Michael OstapThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6085, USA; Center for Engineering MechanoBiology, University of Pennsylvania, Philadelphia, PA 19104-6085, USA. Electronic address: ostap@pennmedicine.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
Molecular Mechanisms of Axonal Transport and Organelle DynamicsR35GM126950 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Erika L Holzbaur · 2018 to 2026
$5.6M
Training in Muscle Biology and Muscle DiseaseT32AR053461 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2006 to 2025
$4.9M
NIAMS NIH HHS T32 AR053461NIGMS NIH HHS P01 GM087253NIGMS NIH HHS R35 GM126950
6 · The paper itself

Abstract

Microtubule and actin filament molecular motors such as kinesin-1 and myosin-Ic (Myo1c) transport and remodel membrane-bound vesicles; however, it is unclear how they coordinate to accomplish these tasks. We introduced kinesin-1- and Myo1c-bound giant unilamellar vesicles (GUVs) into a micropatterned in vitro cytoskeletal matrix modeled after the subcellular architecture where vesicular sorting and membrane remodeling are observed. This array was composed of sparse microtubules intersecting regions dense with actin filaments, and revealed that Myo1c-dependent tethering of GUVs enabled kinesin-1-driven membrane deformation and tubulation. Membrane remodeling at actin/microtubule intersections was modulated by lipid composition and the addition of the Bin-Amphiphysin-Rvs-domain (BAR-domain) proteins endophilin or FCH-domain-only (FCHo). Myo1c not only tethered microtubule-transported cargo, but also transported, deformed, and tubulated GUVs along actin filaments in a lipid-composition- and BAR-protein-responsive manner. These results suggest a mechanism for actin-based involvement in vesicular transport and remodeling of intracellular membranes, and implicate lipid composition as a key factor in determining whether vesicles will undergo transport, deformation, or tubulation driven by opposing actin and microtubule motors and BAR-domain proteins.

Indexed as

Actin CytoskeletonCytoskeletonHumansIntracellular MembranesKinesinsMicrotubulesMyosin Type IKinesinsMyosin Type Iactin filamentBAR proteinendophilinFCHoGUVintracellular transportkinesinmicrotubulemyosintubulationvesicle

Identifiers

PMID29337076
PMCPMC5920771
OpenAlexW2783522701

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.