Evidence map›Paper›PMID 16938849›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

The Nck-interacting kinase phosphorylates ERM proteins for formation of lamellipodium by growth factors.

Martin Baumgartner, Amy L Sillman, Elizabeth M Blackwood, Jyoti Srivastava, Nikki Madson, James W Schilling, Jocelyn H Wright, Diane L Barber

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 10% 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

79 citing papers in PubMed, 1 synthesis or guideline pooled it, 141 citations in OpenAlex.

  1. Pooled it
  2. Trial
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  4. Review
  5. Article
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  16. Ezrin Mediates Invasion and Metastasis in Tumorigenesis: A Review.Frontiers in cell and developmental biology · 2020
    Review
  17. Article
  18. Review
  19. Article
  20. Article

19 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 1 country.

Martin BaumgartnerDepartment of Cell and Tissue Biology, University of California, San Francisco, CA 94143, USA.
Amy L Sillman
Elizabeth M Blackwood
Jyoti Srivastava
Nikki Madson
James W Schilling
Jocelyn H Wright
Diane L Barber
University of California, San Francisco · USMaxygen (United States) · US

Funding

MECHANISMS OF RECEPTOR-REGULATED NA+/H+ EXCHANGER01GM047413 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BARBER, DIANE L · 1993 to 2014
$4.2M
PROGRAM IN CRANIOFACIAL &SKELETAL BIOC06RR016490 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BERTOLAMI, CHARLES N · 2001 to 2001
$2.0M
CELL AND MOLECULAR BASIS OF ORAL BIOLOGYT32DE007204 · NIDCR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI DAMSKY, CAROLINE H · 1989 to 2004
$818k
NCRR NIH HHS C06 RR016490NCRR NIH HHS C06 RR16490NIDCR NIH HHS T32 DE007204NIDCR NIH HHS T32 DE07204NIGMS NIH HHS GM47413NIGMS NIH HHS R01 GM047413
6 · The paper itself

Abstract

The mammalian Ste20-like Nck-interacting kinase (NIK) and its orthologs Misshapen in Drosophila and Mig-15 in Caenorhabditis elegans have a conserved function in regulating cell morphology, although through poorly understood mechanisms. We report two previously unrecognized actions of NIK: regulation of lamellipodium formation by growth factors and phosphorylation of the ERM proteins ezrin, radixin, and moesin. ERM proteins regulate cell morphology and plasma membrane dynamics by reversibly anchoring actin filaments to integral plasma membrane proteins. In vitro assays show that NIK interacts directly with ERM proteins, binding their N termini and phosphorylating a conserved C-terminal threonine. In cells, NIK and phosphorylated ERM proteins localize at the distal margins of lamellipodia, and NIK activity is necessary for phosphorylation of ERM proteins induced by EGF and PDGF, but not by thrombin. Lamellipodium extension in response to growth factors is inhibited in cells expressing a kinase-inactive NIK, suppressed for NIK expression with siRNA oligonucleotides, or expressing ezrin T567A that cannot be phosphorylated. These data suggest that direct phosphorylation of ERM proteins by NIK constitutes a signaling mechanism controlling growth factor-induced membrane protrusion and cell morphology.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCytoskeletal ProteinsEpidermal Growth FactorEzrinGrowth SubstancesIn Vitro TechniquesMembrane ProteinsMiceMicrofilament ProteinsMicroscopy, VideoOncogene ProteinsPhosphorylationPlatelet-Derived Growth FactorProtein BindingPseudopodiaAdaptor Proteins, Signal TransducingCytoskeletal ProteinsEpidermal Growth FactorEzrinGrowth SubstancesMembrane ProteinsMicrofilament ProteinsmoesinNck proteinOncogene ProteinsPlatelet-Derived Growth Factorplatelet-derived growth factor Aradixin

Identifiers

PMID16938849
PMCPMC1569174
OpenAlexW1974651199

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.