Evidence map›Paper›PMID 27535431›Full record

ArticleMolecular biology of the cell2016

Tropomyosin isoforms bias actin track selection by vertebrate myosin Va.

Maria Sckolnick, Elena B Krementsova, David M Warshaw, Kathleen M Trybus

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Actin-tropomyosin distribution in non-muscle cells.Journal of muscle research and cell motility · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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

4 authors at 1 institution in 1 country.

Maria SckolnickDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
Elena B KrementsovaDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
David M WarshawDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
Kathleen M TrybusDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405 kathleen.trybus@uvm.edu.
University of Vermont · US

Funding

MUTATIONAL STUDIES OF PROCESSIVE MYOSIN MOTORSR01GM078097 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 2007 to 2019
$4.8M
Myosin Va Cargo Transport: In Vitro Model SystemsR01GM094229 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI WARSHAW, DAVID M · 2011 to 2020
$2.7M
INVERTED LASER-SCANNING CONFOCAL MICROSCOPE: LUNG RESEARCHS10RR019246 · NCRR · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TAATJES, DOUGLAS J. · 2004 to 2004
$473k
NCRR NIH HHS S10 RR019246NIGMS NIH HHS R01 GM078097NIGMS NIH HHS R01 GM094229
6 · The paper itself

Abstract

Tropomyosin (Tpm) isoforms decorate actin with distinct spatial and temporal localization patterns in cells and thus may function to sort actomyosin processes by modifying the actin track affinity for specific myosin isoforms. We examined the effect of three Tpm isoforms on the ability of myosin Va (myoVa) to engage with actin in vitro in the absence or presence of the cargo adapter melanophilin (Mlph), which links myoVa to Rab27a-melanosomes for in vivo transport. We show that both the myosin motor domain and the cargo adapter Mlph, which has an actin-binding domain that acts as a tether, are sensitive to the Tpm isoform. Actin-Tpm3.1 and actin-Tpm1.8 were equal or better tracks compared to bare actin for myoVa-HMM based on event frequency, run length, and speed. The full-length myoVa-Mlph complex showed high-frequency engagement with actin-Tpm3.1 but not with actin-Tpm1.8. Actin-Tpm4.2 excluded both myoVa-HMM and full-length myoVa-Mlph from productive interactions. Of importance, Tpm3.1 is enriched in the dendritic protrusions and cortical actin of melanocytes, where myoVa-Mlph engages in melanosome transport. These results support the hypothesis that Tpm isoforms constitute an "actin-Tpm code" that allows for spatial and temporal sorting of actomyosin function in the cell.

Indexed as

Actin CytoskeletonActinsActomyosinAdaptor Proteins, Signal TransducingAnimalsBiological TransportCytoskeletal ProteinsHumansMelanocytesMelanosomesMiceMyosin Heavy ChainsMyosinsMyosin Type VProtein BindingProtein IsoformsActinsActomyosinAdaptor Proteins, Signal TransducingCytoskeletal ProteinsMlph protein, mouseMyosin Heavy ChainsMyosinsMyosin Type VProtein IsoformsTropomyosin

Identifiers

PMID27535431
PMCPMC5042576
OpenAlexW2517203162

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.