Evidence map›Paper›PMID 22084092›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Effects of brefeldin A-inhibited guanine nucleotide-exchange (BIG) 1 and KANK1 proteins on cell polarity and directed migration during wound healing.

Chun-Chun Li, Jean-Cheng Kuo, Clare M Waterman, Ryoiti Kiyama, 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, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

27 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. The Protective Role of KANK1 in Podocyte Injury.International journal of molecular sciences · 2024
    Article
  3. Article
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  15. Review
  16. Article
  17. 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
  18. Article
  19. Review
  20. 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

6 authors at 3 institutions in 3 countries.

Chun-Chun LiCardiovascular and Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Jean-Cheng Kuo
Clare M Waterman
Ryoiti Kiyama
Joel Moss
Martha Vaughan
National Institutes of Health · USNational Heart Lung and Blood Institute · USNational Institute of Advanced Industrial Science and Technology · JP

Funding

Mechanical Regulation of Cell AdhesionZIAHL005104 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI WATERMAN, CLARE MICHAL · 2009 to 2025
$30.9M
Light Microscopy CoreZICHL006019 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI COMBS, CHRISTIAN · 2009 to 2025
$29.3M
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 protein (BIG) 1 activates class I ADP ribosylation factors (ARFs) by accelerating the replacement of bound GDP with GTP to initiate recruitment of coat proteins for membrane vesicle formation. Among proteins that interact with BIG1, kinesin family member 21A (KIF21A), a plus-end-directed motor protein, moves cargo away from the microtubule-organizing center (MTOC) on microtubules. Because KANK1, a protein containing N-terminal KN, C-terminal ankyrin-repeat, and intervening coiled-coil domains, has multiple actions in cells and also interacts with KIF21A, we explored a possible interaction between it and BIG1. We obtained evidence for a functional and physical association between these proteins, and found that the effects of BIG1 and KANK1 depletion on cell migration in wound-healing assays were remarkably similar. Treatment of cells with BIG1- or KANK1-specific siRNA interfered significantly with directed cell migration and initial orientation of Golgi/MTOC toward the leading edge, which was not mimicked by KIF21A depletion. Although colocalization of overexpressed KANK1 and endogenous BIG1 in HeLa cells was not clear microscopically, their reciprocal immunoprecipitation (IP) is compatible with the presence of small percentages of each protein in the same complexes. Depletion or overexpression of BIG1 protein appeared not to affect KANK1 distribution. Our data identify actions of both BIG1 and KANK1 in regulating cell polarity during directed migration; these actions are consistent with the presence of both BIG1 and KANK1 in dynamic multimolecular complexes that maintain Golgi/MTOC orientation, differ from those that might contain all three proteins (BIG1, KIF21A, and KANK1), and function in directed transport along microtubules.

Indexed as

Adaptor Proteins, Signal TransducingBlotting, WesternCell MovementCell PolarityCytoskeletal ProteinsGuanine Nucleotide Exchange FactorsHeLa CellsHumansImmunoprecipitationKinesinsMicroscopy, FluorescenceRNA InterferenceRNA, Small InterferingTumor Suppressor ProteinsWound HealingAdaptor Proteins, Signal TransducingARFGEF1 protein, humanCytoskeletal ProteinsGuanine Nucleotide Exchange FactorsKANK1 protein, humanKIF21A protein, humanKinesinsRNA, Small InterferingTumor Suppressor Proteins

Identifiers

PMID22084092
PMCPMC3228443
OpenAlexW1983174249

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.