Evidence map›Paper›PMID 21921029›Full record

ArticleThe Journal of biological chemistry2011

A three-part signal governs differential processing of Gli1 and Gli3 proteins by the proteasome.

Erin K Schrader, Kristine G Harstad, Robert A Holmgren, Andreas Matouschek

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. GLI3: a mediator of genetic diseases, development and cancer.Cell communication and signaling : CCS · 2020
    Review
  9. Biochemical mechanisms of vertebrate hedgehog signaling.Development (Cambridge, England) · 2019
    Review
  10. Review
  11. Article
  12. Article
  13. New insight into the interaction of TRAF2 C-terminal domain with lipid raft microdomains.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. G-protein-coupled receptors, Hedgehog signaling and primary cilia.Seminars in cell & developmental biology · 2014
    Review
  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

4 authors at 1 institution in 1 country.

Erin K SchraderDepartment of Molecular Biosciences and the Robert H. Lurie Comprehensive Cancer Center, Northwestern University, Evanston, Illinois 60208, USA.
Kristine G Harstad
Robert A Holmgren
Andreas Matouschek
Northwestern University · US

Funding

SUPPRESSIVE ROLE OF ANDROGEN RESPONSE GENE CALRETICULIN IN PROSTATE CANCERP50CA090386 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CRAWFORD, SUSAN · 2001 to 2013
$25.1M
TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI O'HALLORAN, THOMAS V · 2009 to 2013
$12.8M
TRAINING PROGRAM IN ONCOGENESIS &DEVELOPMENT BIOLOGYT32CA080621 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI EKLUND, ELIZABETH ANN · 2001 to 2018
$4.1M
Protein unfolding in a physiological systemR01GM063004 · NIGMS · NORTHWESTERN UNIVERSITY · PI MATOUSCHEK, ANDREAS · 2001 to 2012
$2.7M
NCI NIH HHS P50 CA090386NCI NIH HHS P50CA090386NCI NIH HHS T32 CA080621NCI NIH HHS U54 CA143869NIGMS NIH HHS R01 GM063004NIGMS NIH HHS R01GM63004
6 · The paper itself

Abstract

The Gli proteins are the transcriptional effectors of the mammalian Hedgehog signaling pathway. In an unusual mechanism, the proteasome partially degrades or processes Gli3 in the absence of Hedgehog pathway stimulation to create a Gli3 fragment that opposes the activity of the full-length protein. In contrast, Gli1 is not processed but degraded completely, despite considerable homology with Gli3. We found that these differences in processing can be described by defining a processing signal that is composed of three parts: the zinc finger domain, an adjacent linker sequence, and a degron. Gli3 processing is inhibited when any one component of the processing signal is disrupted. We show that the zinc fingers are required for processing only as a folded structure and that the location but not the identity of the processing degron is critical. Within the linker sequence, regions of low sequence complexity play a crucial role, but other sequence features are also important. Gli1 is not processed because two components of the processing signal, the linker sequence and the degron, are ineffective. These findings provide new insights into the molecular elements that regulate Gli protein processing by the proteasome.

Indexed as

ProteolysisHEK293 CellsHumansKruppel-Like Transcription FactorsNerve Tissue ProteinsProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalSignal TransductionTranscription FactorsZinc Finger Protein GLI1Zinc Finger Protein Gli3Zinc FingersGLI1 protein, humanGLI3 protein, humanKruppel-Like Transcription FactorsNerve Tissue ProteinsProteasome Endopeptidase ComplexTranscription FactorsZinc Finger Protein GLI1Zinc Finger Protein Gli3

Identifiers

PMID21921029
PMCPMC3234730
OpenAlexW2001161463

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.