Evidence map›Paper›PMID 26801966›Full record

ArticleCytoskeleton (Hoboken, N.J.)2016

Selective localization of myosin-I proteins in macropinosomes and actin waves.

Hanna Brzeska, Hilary Koech, Kevin J Pridham, Edward D Korn, Margaret A Titus

Abstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  5. Review
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  7. A CIE change in our understanding of endocytic mechanisms.Frontiers in cell and developmental biology · 2023
    Review
  8. Article
  9. Article
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  16. Article
  17. The origins and evolution of macropinocytosis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Review
  18. Article
  19. Article
  20. A Diaphanous-related formin links Ras signaling directly to actin assembly in macropinocytosis and phagocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

5 authors at 3 institutions in 1 country.

Hanna BrzeskaLaboratory of Cell Biology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland.
Hilary KoechLaboratory of Cell Biology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland.
Kevin J PridhamLaboratory of Cell Biology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland.
Edward D KornLaboratory of Cell Biology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland.
Margaret A TitusDepartment of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, Minnesota.
National Heart Lung and Blood Institute · USNational Institutes of Health · USUniversity of Minnesota · US

Funding

Molecular Basis of Dynamic Localization of Class-I MyosinsZIAHL006035 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KORN, EDWARD D · 2010 to 2016
$4.4M
Intramural NIH HHS Z99 HL999999
6 · The paper itself

Abstract

Class I myosins are widely expressed with roles in endocytosis and cell migration in a variety of cell types. Dictyostelium express multiple myosin Is, including three short-tailed (Myo1A, Myo1E, Myo1F) and three long-tailed (Myo1B, Myo1C, Myo1D). Here we report the molecular basis of the specific localizations of short-tailed Myo1A, Myo1E, and Myo1F compared to our previously determined localization of long-tailed Myo1B. Myo1A and Myo1B have common and unique localizations consistent with the various features of their tail region; specifically the BH sites in their tails are required for their association with the plasma membrane and heads are sufficient for relocalization to the front of polarized cells. Myo1A does not localize to actin waves and macropinocytic protrusions, in agreement with the absence of a tail region which is required for these localizations of Myo1B. However, in spite of the overall similarity of their domain structures, the cellular distributions of Myo1E and Myo1F are quite different from Myo1A. Myo1E and Myo1F, but not Myo1A, are associated with macropinocytic cups and actin waves. The localizations of Myo1E and Myo1F in macropinocytic structures and actin waves differ from the localization of Myo1B. Myo1B colocalizes with F-actin in the actin waves and at the tips of mature macropinocytic cups whereas Myo1E and Myo1F are in the interior of actin waves and along the entire surface of macropinocytic cups. Our results point to different mechanisms of targeting of short- and long-tailed myosin Is, and are consistent with these myosins having both shared and divergent cellular functions.

Indexed as

PinocytosisActinsCell MembraneDictyosteliumEndosomesFluorescenceGreen Fluorescent ProteinsMutant ProteinsMyosin Type IProtein Structure, TertiaryProtein TransportProtozoan ProteinsPseudopodiaActinsGreen Fluorescent ProteinsMutant ProteinsMyosin Type IProtozoan Proteinsactin wavesBH sitemacropinocytosismembrane bindingunconventional myosins

Identifiers

PMID26801966
PMCPMC4769671
OpenAlexW2297070012

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.