Evidence map›Paper›PMID 17264123›Full record

ArticleNucleic acids research2007

Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity.

Pierre-Jacques Hamard, Michaël Boyer-Guittaut, Barbara Camuzeaux, Denis Dujardin, Charlotte Hauss, Thomas Oelgeschläger, Marc Vigneron, Claude Kedinger, Bruno Chatton

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Role of ATF7-TAF12 interactions in the vitamin D response hypersensitivity of osteoclast precursors in Paget's disease.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2013
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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 1 institution in 1 country.

Pierre-Jacques HamardInstitut Gilbert Laustriat, Ecole Supérieure de Biotechnologie de Strasbourg, UMR7175 CNRS-ULP, BP10413, 67412 Strasbourg Illkirch Cedex, France.
Michaël Boyer-Guittaut
Barbara Camuzeaux
Denis Dujardin
Charlotte Hauss
Thomas Oelgeschläger
Marc Vigneron
Claude Kedinger
Bruno Chatton
École Normale Supérieure - PSL · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Over the past few years, small ubiquitin-like modifier (SUMO) modification has emerged as an important regulator of diverse pathways and activities including protein localization and transcriptional regulation. We identified a consensus sumoylation motif (IKEE), located within the N-terminal activation domain of the ATF7 transcription factor and thus investigated the role of this modification. ATF7 is a ubiquitously expressed transcription factor, homologous to ATF2, that binds to CRE elements within specific promoters. This protein is able to heterodimerize with Jun or Fos proteins and its transcriptional activity is mediated by interaction with TAF12, a subunit of the general transcription factor TFIID. In the present article, we demonstrate that ATF7 is sumoylated in vitro (using RanBP2 as a E3-specific ligase) and in vivo. Moreover, we show that ATF7 sumoylation affects its intranuclear localization by delaying its entry into the nucleus. Furthermore, SUMO conjugation inhibits ATF7 transactivation activity by (i) impairing its association with TAF12 and (ii) blocking its binding-to-specific sequences within target promoters.

Indexed as

Protein Processing, Post-TranslationalActivating Transcription FactorsCell LineCell NucleusHumansMolecular ChaperonesNuclear Pore Complex ProteinsSUMO-1 ProteinUbiquitin-Protein LigasesActivating Transcription FactorsATF7 protein, humanMolecular ChaperonesNuclear Pore Complex Proteinsran-binding protein 2SUMO-1 ProteinUbiquitin-Protein Ligases

Identifiers

PMID17264123
PMCPMC1851647
OpenAlexW2080047282

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.