Evidence map›Paper›PMID 25278022›Full record

ArticleThe Journal of biological chemistry2014

The E3 ubiquitin ligase MID1 catalyzes ubiquitination and cleavage of Fu.

Susann Schweiger, Stephanie Dorn, Melanie Fuchs, Andrea Köhler, Frank Matthes, Eva-Christina Müller, Erich Wanker, Rainer Schneider, Sybille Krauß

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. mExperimental & molecular medicine · 2026
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  3. Absence of the RING domain inLife science alliance · 2024
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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

9 authors at 5 institutions in 2 countries.

Susann SchweigerInstitute for Human Genetics, Medical School, University of Mainz, 55122 Mainz, Germany.
Stephanie DornGerman Center for Neurodegenerative Diseases, 53127 Bonn, Germany.
Melanie FuchsDepartment of Dermatology, Charité University Hospital, 10117 Berlin, Germany.
Andrea KöhlerInstitute of Biochemistry and Center for Molecular Biosciences Innsbruck, 6020 Innsbruck, Austria, and.
Frank MatthesGerman Center for Neurodegenerative Diseases, 53127 Bonn, Germany.
Eva-Christina MüllerMax Delbrück Center for Molecular Medicine, 13125 Berlin-Buch, Germany.
Erich WankerMax Delbrück Center for Molecular Medicine, 13125 Berlin-Buch, Germany.
Rainer SchneiderInstitute of Biochemistry and Center for Molecular Biosciences Innsbruck, 6020 Innsbruck, Austria, and.
Sybille KraußGerman Center for Neurodegenerative Diseases, 53127 Bonn, Germany,. Electronic address: sybille.krauss@dzne.de.
German Center for Neurodegenerative Diseases · DEMax Delbrück Center · DEUniversität Innsbruck · ATCharité - Universitätsmedizin Berlin · DEJohannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SHH (Sonic Hedgehog)-GLI signaling plays an important role during embryogenesis and in tumorigenesis. The survival and growth of several types of cancer depend on autonomously activated SHH-GLI signaling. A protein complex containing the ubiquitin ligase MID1 and protein phosphatase 2A regulates the nuclear localization and transcriptional activity of GLI3, a transcriptional effector molecule of SHH, in cancer cell lines with autonomously activated SHH signaling. However, the exact molecular mechanisms that mediate the interaction between MID1 and GLI3 remained unknown. Here, we show that MID1 catalyzes the ubiquitination and proteasomal cleavage of the GLI3 regulator Fu. Our data suggest that Fu ubiquitination and cleavage is one of the key elements connecting the MID1-PP2A protein complex with GLI3 activity control.

Indexed as

CatalysisCell Line, TumorCell NucleusDNA PrimersGene Expression Regulation, NeoplasticHedgehog ProteinsHeLa CellsHumansKruppel-Like Transcription FactorsLysineMicrotubule ProteinsNerve Tissue ProteinsNuclear ProteinsProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesSignal TransductionDNA PrimersGLI3 protein, humanHedgehog ProteinsKruppel-Like Transcription FactorsLysineMicrotubule ProteinsMID1 protein, humanNerve Tissue ProteinsNuclear ProteinsProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesSHH protein, humanSTK36 protein, humanTranscription FactorsUbiquitinUbiquitin-Protein LigasesZinc Finger Protein Gli3Cancer BiologyFuGLI3MID1Proteasomal CleavageProteasomeProtein Phosphatase 2 (PP2A)Signal transductionUbiquitination

Identifiers

PMID25278022
PMCPMC4231658
OpenAlexW2041194506

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.