Evidence map›Paper›PMID 25482893›Full record

ArticleRNA biology2014

A single molecule approach to mRNA transport by a class V myosin.

Thomas E Sladewski, Kathleen M Trybus

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 32% 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

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018
    Review
  5. Article
  6. Review
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

2 authors at 1 institution in 1 country.

Thomas E Sladewskia Department of Molecular Physiology & Biophysics ; University of Vermont ; Burlington , VT USA.
Kathleen M Trybus
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
NIGMS NIH HHS GM078097
6 · The paper itself

Abstract

mRNA localization ensures correct spatial and temporal control of protein synthesis in the cell. We show that an in vitro single molecule approach, using purified recombinant full-length proteins and synthesized mRNA, provides insight into the mechanism by which localizing mRNAs are carried to their destination. A messenger ribonucleoprotein (mRNP) complex was reconstituted from a budding yeast class V myosin motor complex (Myo4p-She3p), an mRNA-binding adaptor protein (She2p), and a localizing mRNA (ASH1). The motion of the mRNP was tracked with high spatial (∼10 nm) and temporal (70 ms) resolution. Using this "bottom-up" methodology, we show that mRNA triggers the assembly of a high affinity double-headed motor-mRNA complex that moves continuously for long distances on actin filaments at physiologic ionic strength. Without mRNA, the myosin is monomeric and unable to move continuously on actin. This finding reveals an elegant strategy to ensure that only cargo-bound motors are activated for transport. Increasing the number of localization elements ("zip codes") in the mRNA enhanced both the frequency of motile events and their run length, features which likely enhance cellular localization. Future in vitro reconstitution of mRNPs with kinesin and dynein motors should similarly yield mechanistic insight into mRNA transport by microtubule-based motors.

Indexed as

Actin CytoskeletonActinsMyosin Heavy ChainsMyosin Type VProtein BindingRepressor ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerRNA TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsASH1 protein, S cerevisiaemessenger ribonucleoproteinMyo4 protein, S cerevisiaeMyosin Heavy ChainsMyosin Type VRepressor ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsSHE2 protein, S cerevisiaeSHE3 protein, S cerevisiaeASH1 mRNAmessenger ribonucleoproteinmRNA localizationmRNA transportmRNP, messenger ribonucleoproteinMyo4pShe2pShe3p

Identifiers

PMID25482893
PMCPMC4615833
OpenAlexW2082350401

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.