Evidence map›Paper›PMID 35594862›Full record

ArticleCurrent biology : CB2022

MARK2 regulates directed cell migration through modulation of myosin II contractility and focal adhesion organization.

Ana M Pasapera, Sarah M Heissler, Masumi Eto, Yukako Nishimura, Robert S Fischer, Hawa R Thiam, Clare M Waterman

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2022. 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
4.4field-weighted citation impact, top 4% 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. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Contractile forces direct the chiral swirling of minimal cell collectives.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. TEX38 localizes ZDHHC19 to the plasma membrane and regulates sperm head morphogenesis in mice.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. When everything is a master regulator, nothing is.Molecular biology of the cell · 2025
    Review
  12. Article
  13. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  14. Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry.International journal of molecular sciences · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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

7 authors at 3 institutions in 2 countries.

Ana M PasaperaCell Biology and Physiology Center, National Heart, Lung and Blood Institute, National Institutes of Health, Building 50, South Drive, Room 4537, MSC 8019, Bethesda, MD 20892, USA.
Sarah M HeisslerCell Biology and Physiology Center, National Heart, Lung and Blood Institute, National Institutes of Health, Building 50, South Drive, Room 4537, MSC 8019, Bethesda, MD 20892, USA; Department of Physiology and Cell Biology, The Ohio State University College of Medicine, 370 W. 9th Avenue, Columbus, OH 43210, USA.
Masumi EtoDepartment of Veterinary Medicine, Okayama University of Science, 1-3 Ikoino-oka, Imabari, Ehime 794-8555, Japan.
Yukako NishimuraCell Biology and Physiology Center, National Heart, Lung and Blood Institute, National Institutes of Health, Building 50, South Drive, Room 4537, MSC 8019, Bethesda, MD 20892, USA; Division of Developmental Physiology, Institute for Genetic Medicine, Hokkaido University, Kita 15, Nishi 7, Kita-Ku, Sapporo, Hokkaido 060-0815, Japan.
Robert S FischerCell Biology and Physiology Center, National Heart, Lung and Blood Institute, National Institutes of Health, Building 50, South Drive, Room 4537, MSC 8019, Bethesda, MD 20892, USA.
Hawa R ThiamCell Biology and Physiology Center, National Heart, Lung and Blood Institute, National Institutes of Health, Building 50, South Drive, Room 4537, MSC 8019, Bethesda, MD 20892, USA.
Clare M WatermanCell Biology and Physiology Center, National Heart, Lung and Blood Institute, National Institutes of Health, Building 50, South Drive, Room 4537, MSC 8019, Bethesda, MD 20892, USA. Electronic address: watermancm@nhlbi.nih.gov.
National Institutes of Health · USNational Heart Lung and Blood Institute · USOkayama University of Science · JP

Funding

Integration of Actin Dynamics and Adhesion in Cell MigrationZIAHL005105 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI WATERMAN, CLARE MICHAL · 2009 to 2025
$16.5M
Molecular Mechanisms of Myosin-3R01GM143414 · NIGMS · OHIO STATE UNIVERSITY · PI HEISSLER, SARAH · 2021 to 2025
$1.7M
Integration of Actin Dynamics and Adhesion in Cell MigrationZ01HL005105 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI WATERMAN, CLARE MICHAL · 2008 to 2008
$681k
Intramural NIH HHS Z01 HL005105NIGMS NIH HHS R01 GM143414
6 · The paper itself

Abstract

Cancer cell migration during metastasis is mediated by a highly polarized cytoskeleton. MARK2 and its invertebrate homolog Par1B are kinases that regulate the microtubule cytoskeleton to mediate polarization of neurons in mammals and embryos in invertebrates. However, the role of MARK2 in cancer cell migration is unclear. Using osteosarcoma cells, we found that in addition to its known localizations on microtubules and the plasma membrane, MARK2 also associates with the actomyosin cytoskeleton and focal adhesions. Cells depleted of MARK proteins demonstrated that MARK2 promotes phosphorylation of both myosin II and the myosin phosphatase targeting subunit MYPT1 to synergistically drive myosin II contractility and stress fiber formation in cells. Studies with isolated proteins showed that MARK2 directly phosphorylates myosin II regulatory light chain, while its effects on MYPT1 phosphorylation are indirect. Using a mutant lacking the membrane-binding domain, we found that membrane association is required for focal adhesion targeting of MARK2, where it specifically enhances cell protrusion by promoting FAK phosphorylation and formation of focal adhesions oriented in the direction of migration to mediate directionally persistent cell motility. Together, our results define MARK2 as a master regulator of the actomyosin and microtubule cytoskeletal systems and focal adhesions to mediate directional cancer cell migration.

Indexed as

ActomyosinFocal AdhesionsAnimalsCell AdhesionCell MovementMammalsMyosin Light ChainsMyosin Type IIPhosphorylationActomyosinMyosin Light ChainsMyosin Type IIcell polaritydirected cell migrationMARK2Myosin IIMYPT1Par1b

Identifiers

PMID35594862
PMCPMC9354676
OpenAlexW4280591028

What OpenQuestion holds

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Registered trials

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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.