Evidence map›Paper›PMID 10669731›Full record

ArticleMolecular and cellular biology2000

Nck-interacting Ste20 kinase couples Eph receptors to c-Jun N-terminal kinase and integrin activation.

E Becker, U Huynh-Do, S Holland, T Pawson, T O Daniel, E Y Skolnik

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

56 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Review
  3. Sinner or Saint?: Nck Adaptor Proteins in Vascular Biology.Frontiers in cell and developmental biology · 2021
    Review
  4. Article
  5. Article
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  7. Review
  8. Article
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  12. Review
  13. Cell segregation in the vertebrate hindbrain: a matter of boundaries.Cellular and molecular life sciences : CMLS · 2015
    Review
  14. Article
  15. The C. elegans NR4A nuclear receptor gene nhr-6 promotes cell cycle progression in the spermatheca lineage.Developmental dynamics : an official publication of the American Association of Anatomists · 2015
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  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 2 countries.

E BeckerDepartment of Pharmacology, Skirball Institute of Biomolecular Medicine, New York University Medical Center, New York, New York 10016, USA.
U Huynh-Do
S Holland
T Pawson
T O Daniel
E Y Skolnik
Cornell University · USLunenfeld-Tanenbaum Research Institute · CAVanderbilt University Medical Center · US

Funding

SIGNALS FOR RENAL ENDOTHELIAL CAPILLARY MORPHOGENESISR01DK047078 · NIDDK · VANDERBILT UNIVERSITY · PI CHEN, JIN · 1994 to 2001
$389k
INSULIN RECEPTOR SIGNALING--ROLE IN NIDDMR01DK049207 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SKOLNIK, EDWARD Y · 1995 to 2001
$244k
NIDDK NIH HHS DK47078NIDDK NIH HHS DK49207
6 · The paper itself

Abstract

The mammalian Ste20 kinase Nck-interacting kinase (NIK) specifically activates the c-Jun amino-terminal kinase (JNK) mitogen-activated protein kinase module. NIK also binds the SH3 domains of the SH2/SH3 adapter protein Nck. To determine whether Nck functions as an adapter to couple NIK to a receptor tyrosine kinase signaling pathway, we determined whether NIK is activated by Eph receptors (EphR). EphRs constitute the largest family of receptor tyrosine kinases (RTK), and members of this family play important roles in patterning of the nervous and vascular systems. In this report, we show that NIK kinase activity is specifically increased in cells stimulated by two EphRs, EphB1 and EphB2. EphB1 kinase activity and phosphorylation of a juxtamembrane tyrosine (Y594), conserved in all Eph receptors, are both critical for NIK activation by EphB1. Although pY594 in the EphB1R has previously been shown to bind the SH2 domain of Nck, we found that stimulation of EphB1 and EphB2 led predominantly to a complex between NIK/Nck, p62(dok), RasGAP, and an unidentified 145-kDa tyrosine-phosphorylated protein. Tyrosine-phosphorylated p62(dok) most probably binds directly to the SH2 domain of Nck and RasGAP and indirectly to NIK bound to the SH3 domain of Nck. We found that NIK activation is also critical for coupling EphB1R to biological responses that include the activation of integrins and JNK by EphB1. Taken together, these findings support a model in which the recruitment of the Ste20 kinase NIK to phosphotyrosine-containing proteins by Nck is an important proximal step in the signaling cascade downstream of EphRs.

Indexed as

Saccharomyces cerevisiae ProteinsSignal TransductionAdaptor Proteins, Signal TransducingAnimalsCell LineIntegrinsIntracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase KinasesMitogen-Activated Protein KinasesOncogene ProteinsProtein Serine-Threonine KinasesReceptor Protein-Tyrosine KinasesAdaptor Proteins, Signal TransducingIntegrinsIntracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase KinasesMitogen-Activated Protein KinasesNck proteinOncogene ProteinsProtein Serine-Threonine KinasesReceptor Protein-Tyrosine KinasesSaccharomyces cerevisiae ProteinsSTE20 protein, S cerevisiae

Identifiers

PMID10669731
PMCPMC85333
OpenAlexW2138747143

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.