Evidence map›Paper›PMID 24214986›Full record

ArticleThe Journal of biological chemistry2013

Myosin 3A kinase activity is regulated by phosphorylation of the kinase domain activation loop.

Omar A Quintero, William C Unrath, Stanley M Stevens, Uri Manor, Bechara Kachar, Christopher M Yengo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 32 citations in OpenAlex.

  1. Trial
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  13. Review
  14. Functional Role of Class III Myosins in Hair Cells.Frontiers in cell and developmental biology · 2021
    Review
  15. Review
  16. Article
  17. Article
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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

6 authors at 4 institutions in 1 country.

Omar A QuinteroFrom the Department of Cellular and Molecular Physiology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033.
William C Unrath
Stanley M Stevens
Uri Manor
Bechara Kachar
Christopher M Yengo
National Institute on Deafness and Other Communication Disorders · USPennsylvania State University · USPenn State Milton S. Hershey Medical Center · USUniversity of South Florida · US

Funding

Structural and Molecular Basis of Transduction in Auditory Sensory OrgansZIADC000002 · NIDCD · NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS · PI KACHAR, BECHARA · 2009 to 2025
$38.3M
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 EY0181416NEI NIH HHS R01 EY018141
6 · The paper itself

Abstract

Class III myosins are unique members of the myosin superfamily in that they contain both a motor and kinase domain. We have found that motor activity is decreased by autophosphorylation, although little is known about the regulation of the kinase domain. We demonstrate by mass spectrometry that Thr-178 and Thr-184 in the kinase domain activation loop and two threonines in the loop 2 region of the motor domain are autophosphorylated (Thr-908 and Thr-919). The kinase activity of MYO3A 2IQ with the phosphomimic (T184E) or phosphoblock (T184A) mutations demonstrates that kinase activity is reduced 30-fold as a result of the T184A mutation, although the Thr-178 site only had a minor impact on kinase activity. Interestingly, the actin-activated ATPase activity of MYO3A 2IQ is slightly reduced as a result of the T178A and T184A mutations suggesting coupling between motor and kinase domains. Full-length GFP-tagged T184A and T184E MYO3A constructs transfected into COS7 cells do not disrupt the ability of MYO3A to localize to filopodia structures. In addition, we demonstrate that T184E MYO3A reduces filopodia elongation in the presence of espin-1, whereas T184A enhances filopodia elongation in a similar fashion to kinase-dead MYO3A. Our results suggest that as MYO3A accumulates at the tips of actin protrusions, autophosphorylation of Thr-184 enhances kinase activity resulting in phosphorylation of the MYO3A motor and reducing motor activity. The differential regulation of the kinase and motor activities allows for MYO3A to precisely self-regulate its concentration in the actin bundle-based structures of cells.

Indexed as

ActinsAdaptor Proteins, Vesicular TransportAmino Acid SubstitutionAnimalsChlorocebus aethiopsCOS CellsHumansMutation, MissenseMyosin Heavy ChainsMyosin Type IIIPhosphorylationProtein Structure, TertiaryPseudopodiaSf9 CellsSpodopteraActinsAdaptor Proteins, Vesicular TransportepsinMYO3A protein, humanMyosin Heavy ChainsMyosin Type IIIActinHearingMolecular MotorsMyosinPhosphorylation

Identifiers

PMID24214986
PMCPMC3873568
OpenAlexW2026948241

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.