Evidence map›Paper›PMID 22578841›Full record

ArticleMolecular cell2012

An acetylation switch regulates SUMO-dependent protein interaction networks.

Rebecca Ullmann, Christopher D Chien, Maria Laura Avantaggiati, Stefan Muller

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

51 citing papers in PubMed, 93 citations in OpenAlex.

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  17. SUMO: From Bench to Bedside.Physiological reviews · 2020
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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

4 authors at 3 institutions in 2 countries.

Rebecca UllmannInstitute of Biochemistry II, Goethe University School of Medicine, Theodor-Stern-Kai 7, D-60590 Frankfurt, Germany.
Christopher D Chien
Maria Laura Avantaggiati
Stefan Muller
Georgetown University Medical Center · USGoethe University Frankfurt · DEMax Planck Institute of Biochemistry · DE

Funding

Georgetown-Howard Universities Center for Clinical and Translational Science (GHUUL1TR000101 · NCATS · GEORGETOWN UNIVERSITY · PI MELLMAN, THOMAS A, VERBALIS, JOSEPH G · 2012 to 2015
$19.3M
TRAINING GRANT IN TUMOR BIOLOGYT32CA009686 · NCI · GEORGETOWN UNIVERSITY · PI ANNA Tate RIEGEL, DAVID J ROBBINS · 1996 to 2026
$10.8M
anti-tumor activity of deactylase inhibitorsR01CA102746 · NCI · GEORGETOWN UNIVERSITY · PI AVANTAGGIATI, MARIA L · 2004 to 2008
$1.4M
ACETYLTRANSFERASES AND ONCOGENESISR01CA083979 · NCI · ROSWELL PARK CANCER INSTITUTE CORP · PI AVANTAGGIATI, MARIA L · 1999 to 2003
$839k
Functional Mimicry of the p53 C-terminal Tail by the Ubiquitin-like Molecule SUMOR21CA123234 · NCI · GEORGETOWN UNIVERSITY · PI AVANTAGGIATI, MARIA L · 2008 to 2009
$380k
NCATS NIH HHS UL1 TR000101NCI NIH HHS R01 CA083979NCI NIH HHS R01 CA102746NCI NIH HHS R21 CA123234NCI NIH HHS R21CA123234NCI NIH HHS T32 CA009686
6 · The paper itself

Abstract

The attachment of the SUMO modifier to proteins controls cellular signaling pathways through noncovalent binding to SUMO-interaction motifs (SIMs). Canonical SIMs contain a core of hydrophobic residues that bind to a hydrophobic pocket on SUMO. Negatively charged residues of SIMs frequently contribute to binding by interacting with a basic surface on SUMO. Here we define acetylation within this basic interface as a central mechanism for the control of SUMO-mediated interactions. The acetyl-mediated neutralization of basic charges on SUMO prevents binding to SIMs in PML, Daxx, and PIAS family members but does not affect the interaction between RanBP2 and SUMO. Acetylation is controlled by HDACs and attenuates SUMO- and PIAS-mediated gene silencing. Moreover, it affects the assembly of PML nuclear bodies and restrains the recruitment of the corepressor Daxx to these structures. This acetyl-dependent switch thus expands the regulatory repertoire of SUMO signaling and determines the selectivity and dynamics of SUMO-SIM interactions.

Indexed as

Protein Interaction MapsAcetylationBinding SitesGene SilencingHEK293 CellsHeLa CellsHistone DeacetylasesHumansSUMO-1 ProteinHistone DeacetylasesSUMO-1 Protein

Identifiers

PMID22578841
PMCPMC3614008
OpenAlexW2085752596

What OpenQuestion holds

Textmetadata
LicenceTDM
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.