Evidence map›Paper›PMID 23568824›Full record

ArticleCytoskeleton (Hoboken, N.J.)2013

Biochemical and bioinformatic analysis of the myosin-XIX motor domain.

Rebecca C Adikes, William C Unrath, Christopher M Yengo, Omar A Quintero

Open access · greenAbstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2013. 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
1.4field-weighted citation impact, top 17% 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, 27 citations in OpenAlex.

  1. Article
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  5. Article
  6. Adipocyte-specific deletion of HuR induces spontaneous cardiac hypertrophy and fibrosis.American journal of physiology. Heart and circulatory physiology · 2021
    Article
  7. Article
  8. Miro: A molecular switch at the center of mitochondrial regulation.Protein science : a publication of the Protein Society · 2020
    Review
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  12. 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 2 institutions in 1 country.

Rebecca C AdikesProgram in Biochemistry, Mount Holyoke College, South Hadley, Massachusetts, USA.
William C Unrath
Christopher M Yengo
Omar A Quintero
Penn State Milton S. Hershey Medical Center · USMount Holyoke College · US

Funding

Enzymatic and Motor Properties of Myosin IIIR01EY018141 · NEI · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI YENGO, CHRISTOPHER M · 2008 to 2012
$1.3M
Enzymatic and Motor Properties of Myosin 19K01CA160667 · NCI · UNIVERSITY OF RICHMOND · PI QUINTERO-CARMONA, OMAR ALBERTO · 2011 to 2013
$353k
NCI NIH HHS K01 CA160667NCI NIH HHS K01CA160667NEI NIH HHS EY018141NEI NIH HHS R01 EY018141
6 · The paper itself

Abstract

Mitochondrial dynamics are dependent on both the microtubule and actin cytoskeletal systems. Evidence for the involvement of myosin motors has been described in many systems, and until recently a candidate mitochondrial myosin transport motor had not been described in vertebrates. Myosin-XIX (MYO19) was predicted to represent a novel class of myosin and had previously been shown to bind to mitochondria and increase mitochondrial network dynamics when ectopically expressed. Our analyses comparing ∼40 MYO19 orthologs to ∼2000 other myosin motor domain sequences identified instances of homology well-conserved within class XIX myosins that were not found in other myosin classes, suggesting MYO19-specific mechanochemistry. Steady-state biochemical analyses of the MYO19 motor domain indicate that Homo sapiens MYO19 is a functional motor. Insect cell-expressed constructs bound calmodulin as a light chain at the predicted stoichiometry and displayed actin-activated ATPase activity. MYO19 constructs demonstrated high actin affinity in the presence of ATP in actin-co-sedimentation assays, and translocated actin filaments in gliding assays. Expression of GFP-MYO19 containing a mutation impairing ATPase activity did not enhance mitochondrial network dynamics, as occurs with wild-type MYO19, indicating that myosin motor activity is required for mitochondrial motility. The measured biochemical properties of MYO19 suggest it is a high-duty ratio motor that could serve to transport mitochondria or anchor mitochondria, depending upon the cellular microenvironment.

Indexed as

ActinsAdenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceAnimalsCalmodulinCell Line, TumorComputational BiologyHumansMitochondriaMolecular Sequence DataMyosinsProtein BindingProtein Structure, TertiaryActinsAdenosine TriphosphatasesAdenosine TriphosphateCalmodulinMyosins

Identifiers

PMID23568824
PMCPMC3927398
OpenAlexW1491392822

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.