Evidence map›Paper›PMID 23918382›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Arf guanine nucleotide-exchange factors BIG1 and BIG2 regulate nonmuscle myosin IIA activity by anchoring myosin phosphatase complex.

Kang Le, Chun-Chun Li, Guan Ye, Joel Moss, Martha Vaughan

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 34 citations in OpenAlex.

  1. Arf1 and ARFGEF2/Sec71 control neuroblast polarity by anchoring nonmuscle myosin II.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Haploinsufficiency of ARFGEF1 is associated with developmental delay, intellectual disability, and epilepsy with variable expressivity.Genetics in medicine : official journal of the American College of Medical Genetics · 2021
    Article
  3. TheMolecular biology of the cell · 2020
    Article
  4. Article
  5. Article
  6. Arf GAPs and molecular motors.Small GTPases · 2019
    Review
  7. Article
  8. Article
  9. Review
  10. Enhancement of β-catenin activity by BIG1 plus BIG2 via Arf activation and cAMP signals.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Article
  12. Review
  13. 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

5 authors at 2 institutions in 1 country.

Kang LeCardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Chun-Chun Li
Guan Ye
Joel Moss
Martha Vaughan
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Molecular Characterization and Regulation of GTP-binding ProteinsZIAHL000627 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI VAUGHAN, MARTHA · 2009 to 2016
$8.4M
Intramural NIH HHS
6 · The paper itself

Abstract

Brefeldin A-inhibited guanine nucleotide-exchange factors BIG1 and BIG2 activate, through their Sec7 domains, ADP ribosylation factors (Arfs) by accelerating the replacement of Arf-bound GDP with GTP for initiation of vesicular transport or activation of specific enzymes that modify important phospholipids. They are also implicated in regulation of cell polarization and actin dynamics for directed migration. Reciprocal coimmunoprecipitation of endogenous HeLa cell BIG1 and BIG2 with myosin IIA was demonstrably independent of Arf guanine nucleotide-exchange factor activity, because effects of BIG1 and BIG2 depletion were reversed by overexpression of the cognate BIG molecule C-terminal sequence that follows the Arf activation site. Selective depletion of BIG1 or BIG2 enhanced specific phosphorylation of myosin regulatory light chain (T18/S19) and F-actin content, which impaired cell migration in Transwell assays. Our data are clear evidence of these newly recognized functions for BIG1 and BIG2 in transduction or integration of mechanical signals from integrin adhesions and myosin IIA-dependent actin dynamics. Thus, by anchoring or scaffolding the assembly, organization, and efficient operation of multimolecular myosin phosphatase complexes that include myosin IIA, protein phosphatase 1δ, and myosin phosphatase-targeting subunit 1, BIG1 and BIG2 serve to integrate diverse biophysical and biochemical events in cells.

Indexed as

Analysis of VarianceBlotting, WesternCell MovementCell PolarityFluorescent Antibody TechniqueGuanine Nucleotide Exchange FactorsHeLa CellsHumansImmunoprecipitationMyosin-Light-Chain PhosphataseNonmuscle Myosin Type IIAPhosphorylationRNA, Small InterferingARFGEF1 protein, humanARFGEF2 protein, humanGuanine Nucleotide Exchange FactorsMyosin-Light-Chain PhosphataseNonmuscle Myosin Type IIARNA, Small Interfering

Identifiers

PMID23918382
PMCPMC3752278
OpenAlexW2154221570

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.