Evidence map›Paper›PMID 22790203›Full record

ArticleSmall GTPases

IAPs as E3 ligases of Rac1: shaping the move.

Tripat Kaur Oberoi-Khanuja, Krishnaraj Rajalingam

Open access · hybridAbstract read
In one paragraph

Article in Small GTPases. 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
0.7field-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, 20 citations in OpenAlex.

  1. Review
  2. The cross talk of ubiquitination and chemotherapy tolerance in colorectal cancer.Journal of cancer research and clinical oncology · 2024
    Review
  3. Article
  4. Review
  5. Frontiers in physiology · 2021
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Regulating Rho GTPases and their regulators.Nature reviews. Molecular cell biology · 2016
    Review
  11. Article
  12. Small Rho GTPases in the control of cell shape and mobility.Cellular and molecular life sciences : CMLS · 2014
    Review
  13. Review
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

2 authors at 2 institutions in 2 countries.

Tripat Kaur Oberoi-KhanujaEmmy Noether Group of the DFG, Institute of Biochemistry II, Goethe University Medical School; Frankfurt, Germany.
Krishnaraj Rajalingam
Goethe Institute · GBGoethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inhibitors of Apoptosis Proteins (IAPs) are well-studied E3 ubiquitin ligases predominantly known for regulation of apoptosis. We uncovered that IAPs can function as a direct E3 ubiquitin ligase of RhoGTPase Rac1. cIAP1 and XIAP directly conjugate polyubiquitin chains to Lysine 147 of activated Rac1 and target it for proteasomal degradation. Consistently, loss of these IAPs by various strategies led to stabilization of Rac1 and mesenchymal mode of migration in tumor cells. IAPs also regulate Rac1 degradation upon RhoGDI1 depletion and CNF1 toxin treatment. Our observations revealed an evolutionarily conserved role of IAPs in regulating Rac1 stability shedding light on to the mechanisms behind ubiquitination-dependent inactivation of Rac1 signaling.

Indexed as

Cell MovementAnimalsCell ShapeHumansInhibitor of Apoptosis ProteinsNeoplasm MetastasisNeoplasmsrac1 GTP-Binding ProteinUbiquitinUbiquitinationUbiquitin-Protein LigasesX-Linked Inhibitor of Apoptosis ProteinInhibitor of Apoptosis Proteinsrac1 GTP-Binding ProteinUbiquitinUbiquitin-Protein LigasesX-Linked Inhibitor of Apoptosis Protein

Identifiers

PMID22790203
PMCPMC3408978
OpenAlexW1986235349

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.