Evidence map›Paper›PMID 22216226›Full record

ArticlePloS one2011

Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.

Alexander Wolf, Knut Beuerlein, Christoph Eckart, Hendrik Weiser, Beate Dickkopf, Helmut Müller, Hiroaki Sakurai, Michael Kracht

Open access · goldAbstract readValidation Study
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.3field-weighted citation impact, top 32% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Atypical p38 Kinase Signaling in Retinal Vascular Damage and Recovery.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  3. Article
  4. Article
  5. Pseudophosphatases as Regulators of MAPK Signaling.International journal of molecular sciences · 2021
    Review
  6. Atypical p38 Signaling, Activation, and Implications for Disease.International journal of molecular sciences · 2021
    Review
  7. Review
  8. Article
  9. Article
  10. Post-Translational Modifications of the TAK1-TAB Complex.International journal of molecular sciences · 2017
    Review
  11. Article
  12. Article
  13. 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

8 authors at 2 institutions in 2 countries.

Alexander WolfRudolf-Buchheim-Institute of Pharmacology, Justus-Liebig-University Giessen, Giessen, Germany.
Knut Beuerlein
Christoph Eckart
Hendrik Weiser
Beate Dickkopf
Helmut Müller
Hiroaki Sakurai
Michael Kracht
University of Giessen · DEUniversity of Toyama · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TAB1 was defined as a regulatory subunit of the protein kinase TAK1, which functions upstream in the pathways activated by interleukin (IL)-1, tumor necrosis factor (TNF), toll-like receptors (TLRs) and stressors. However, TAB1 also functions in the p38 MAPK pathway downstream of TAK1. We identified amino acids (aa) 452/453 and 456/457 of TAB1 as novel sites phosphorylated by TAK1 as well as by p38 MAPK in intact cells as well as in vitro. Serines 452/453 and 456/457 were phosphorylated upon phosphatase blockade by calyculin A, or in response to IL-1 or translational stressors such as anisomycin and sorbitol. Deletion or phospho-mimetic mutations of aa 452-457 of TAB1 retain TAB1 and p38 MAPK in the cytoplasm. The TAB1 mutant lacking aa 452-457 decreases TAB1-dependent phosphorylation of p38 MAPK. It also enhances TAB1-dependent CCL5 secretion in response to IL-1 and increases activity of a post-transcriptional reporter gene, which contains the CCL5 3' untranslated region. These data suggest a complex role of aa 452-457 of TAB1 in controlling p38 MAPK activity and subcellular localization and implicate these residues in TAK1- or p38 MAPK-dependent post-transcriptional control of gene expression.

Indexed as

Amino Acid SequenceBase SequenceCell LineCytokinesCytoplasmDNA PrimersEnzyme-Linked Immunosorbent AssayHumansIntracellular Signaling Peptides and ProteinsMolecular Sequence DataMutationp38 Mitogen-Activated Protein KinasesPhosphorylationRNA Processing, Post-TranscriptionalSequence Homology, Amino AcidStress, PhysiologicalCytokinesDNA PrimersIntracellular Signaling Peptides and Proteinsp38 Mitogen-Activated Protein KinasesTAB1 protein, MAPKKK activator, vertebrate

Identifiers

PMID22216226
PMCPMC3245275
OpenAlexW2148095388

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.