Evidence map›Paper›PMID 9808624›Full record

ArticleGenes & development1998

JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extension.

Y Xia, Z Wu, B Su, B Murray, M Karin

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

83 citing papers in PubMed, 1 synthesis or guideline pooled it, 202 citations in OpenAlex.

  1. Pooled it
  2. Article
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  8. Article
  9. MKK4 Inhibitors-Recent Development Status and Therapeutic Potential.International journal of molecular sciences · 2023
    Review
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  11. Review
  12. Article
  13. Article
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  15. A cryptic tubulin-binding domain links MEKK1 to curved tubulin protomers.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Review
  17. Review
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  20. Review

23 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

5 authors at 3 institutions in 1 country.

Y XiaLaboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, University of California San Diego, La Jolla, California 92093-0636 USA.
Z Wu
B Su
B Murray
M Karin
SignalRx Pharmaceuticals (United States) · USUniversity of California, San Diego · USThe University of Texas MD Anderson Cancer Center · US

Funding

UNIQUE CARDIOVASCULAR RESPONSE TO STRESSORS AND LINKAGE WITH HYPERTENSIONP01HL035018 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PRINTZ, MORTON P · 1986 to 2007
$14.7M
NHLBI NIH HHS HL 35018NHLBI NIH HHS P01 HL035018
6 · The paper itself

Abstract

MAP kinase (MAPK) cascades are composed of a MAPK, MAPK kinase (MAPKK), and a MAPKK kinase (MAPKKK). Despite the existence of numerous components and ample opportunities for crosstalk, most MAPKs are specifically and distinctly activated. We investigated the basis for specific activation of the JNK subgroup of MAPKs. The specificity of JNK activation is determined by the MAPKK JNKK1, which interacts with the MAPKKK MEKK1 and JNK through its amino-terminal extension. Inactive JNKK1 mutants can disrupt JNK activation by MEKK1 or tumor necrosis factor (TNF) in intact cells only if they contain an intact amino-terminal extension. Mutations in this region interfere with the ability of JNKK1 to respond to TNF but do not affect its activation by physical stressors. As JNK and MEKK1 compete for binding to JNKK1 and activation of JNKK1 prevents its binding to MEKK1, activation of this module is likely to occur through sequential MEKK1:JNKK1 and JNKK1:JNK interactions. These results underscore a role for the amino-terminal extension of MAPKKs in determination of response specificity.

Indexed as

MAP Kinase Kinase 4MAP Kinase Kinase Kinase 1Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesAnimalsBinding, CompetitiveCalcium-Calmodulin-Dependent Protein KinasesCOS CellsEnzyme ActivationHumansJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein Kinase 1p38 Mitogen-Activated Protein KinasesPeptide FragmentsPhosphorylationProtein Serine-Threonine KinasesCalcium-Calmodulin-Dependent Protein KinasesJNK Mitogen-Activated Protein KinasesMAP2K4 protein, humanMAP3K1 protein, humanMAP Kinase Kinase 4MAP Kinase Kinase Kinase 1Mitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein Kinasesp38 Mitogen-Activated Protein KinasesPeptide FragmentsProtein Serine-Threonine KinasesProtein-Tyrosine Kinases

Identifiers

PMID9808624
PMCPMC317229
OpenAlexW2111252945

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.