Evidence map›Paper›PMID 25601402›Full record

ArticleThe Journal of cell biology2015

The Nck-interacting kinase NIK increases Arp2/3 complex activity by phosphorylating the Arp2 subunit.

Lawrence L LeClaire, Manish Rana, Martin Baumgartner, Diane L Barber

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 51 citations in OpenAlex.

  1. Akt-phosphorylated UFL1 UFMylates ArpC4 to promote metastasis.Nature structural & molecular biology · 2025
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  8. [Establishment and Preliminary Analysis of Lung Cancer Cell Line A549 with StableSichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2022
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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

4 authors at 1 institution in 2 countries.

Lawrence L LeClaireDepartment of Cell and Tissue Biology, University of California, San Francisco, San Francisco, CA 94143 Department of Biochemistry and Molecular Biology, University of South Alabama, Mobile, AL 36688 leclaire@southalabama.edu.
Manish RanaDepartment of Cell and Tissue Biology, University of California, San Francisco, San Francisco, CA 94143.
Martin BaumgartnerDepartment of Cell and Tissue Biology, University of California, San Francisco, San Francisco, CA 94143 Neuro-Oncology Laboratory, Infectious Diseases and Cancer Research, University of Children's Hospital Zürich, Zürich, Switzerland CH-8008.
Diane L BarberDepartment of Cell and Tissue Biology, University of California, San Francisco, San Francisco, CA 94143.
University of California, San Francisco · US

Funding

MECHANISMS OF RECEPTOR-REGULATED NA+/H+ EXCHANGER01GM047413 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BARBER, DIANE L · 1993 to 2014
$4.2M
Spinning disk confocal / FRAP microscope for quantitative live cell imagingS10RR026758 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WITTMANN, TORSTEN · 2010 to 2010
$500k
NCRR NIH HHS S10 RR026758NIGMS NIH HHS GM47413NIGMS NIH HHS R01 GM047413
6 · The paper itself

Abstract

The nucleating activity of the Arp2/3 complex promotes the assembly of branched actin filaments that drive plasma membrane protrusion in migrating cells. Arp2/3 complex binding to nucleation-promoting factors of the WASP and WAVE families was previously thought to be sufficient to increase nucleating activity. However, phosphorylation of the Arp2 subunit was recently shown to be necessary for Arp2/3 complex activity. We show in mammary carcinoma cells that mutant Arp2 lacking phosphorylation assembled with endogenous subunits and dominantly suppressed actin filament assembly and membrane protrusion. We also report that Nck-interacting kinase (NIK), a MAP4K4, binds and directly phosphorylates the Arp2 subunit, which increases the nucleating activity of the Arp2/3 complex. In cells, NIK kinase activity was necessary for increased Arp2 phosphorylation and plasma membrane protrusion in response to epidermal growth factor. NIK is the first kinase shown to phosphorylate and increase the activity of the Arp2/3 complex, and our findings suggest that it integrates growth factor regulation of actin filament dynamics.

Indexed as

Protein Processing, Post-TranslationalActin-Related Protein 2ActinsAnimalsCell Line, TumorCell ShapeKineticsNF-kappaB-Inducing KinasePhosphorylationProtein MultimerizationProtein Serine-Threonine KinasesProtein SubunitsPseudopodiaRatsActin-Related Protein 2ActinsNF-kappaB-Inducing KinaseProtein Serine-Threonine KinasesProtein Subunits

Identifiers

PMID25601402
PMCPMC4298681
OpenAlexW2092129375

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.