Evidence map›Paper›PMID 35871297›Full record

ArticleNucleic acids research2022

Zinc controls PML nuclear body formation through regulation of a paralog specific auto-inhibition in SUMO1.

Mathieu Lussier-Price, Haytham M Wahba, Xavier H Mascle, Laurent Cappadocia, Veronique Bourdeau, Christina Gagnon, Sebastian Igelmann, Kazuyasu Sakaguchi, Gerardo Ferbeyre, James G Omichinski

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

6 citing papers in PubMed, 17 citations in OpenAlex.

  1. Discovery of novel murine PML isoforms.Nucleus (Austin, Tex.) · 2026
    Article
  2. Review
  3. Review
  4. Decoding the Implications of Zinc in the Development and Therapy of Leukemia.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  5. Review
  6. 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

10 authors at 3 institutions in 3 countries.

Mathieu Lussier-PriceDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC, Canada.
Haytham M WahbaDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC, Canada.
Xavier H MascleDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC, Canada.
Laurent CappadociaDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC, Canada.
Veronique BourdeauDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC, Canada.
Christina GagnonDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC, Canada.
Sebastian IgelmannDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC, Canada.
Kazuyasu SakaguchiDepartment of Chemistry, Faculty of Science, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-8434-4171
Gerardo FerbeyreDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC, Canada.ORCID 0000-0002-2146-618X
James G OmichinskiDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC, Canada.ORCID 0000-0002-3543-1914
Université de Montréal · CABeni-Suef University · EGHokkaido University · JP

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
CIHR 130414CIHR 166104CIHR 70439NIGMS NIH HHS P41 GM103485
6 · The paper itself

Abstract

SUMO proteins are important regulators of many key cellular functions in part through their ability to form interactions with other proteins containing SUMO interacting motifs (SIMs). One characteristic feature of all SUMO proteins is the presence of a highly divergent intrinsically disordered region at their N-terminus. In this study, we examine the role of this N-terminal region of SUMO proteins in SUMO-SIM interactions required for the formation of nuclear bodies by the promyelocytic leukemia (PML) protein (PML-NBs). We demonstrate that the N-terminal region of SUMO1 functions in a paralog specific manner as an auto-inhibition domain by blocking its binding to the phosphorylated SIMs of PML and Daxx. Interestingly, we find that this auto-inhibition in SUMO1 is relieved by zinc, and structurally show that zinc stabilizes the complex between SUMO1 and a phospho-mimetic form of the SIM of PML. In addition, we demonstrate that increasing cellular zinc levels enhances PML-NB formation in senescent cells. Taken together, these results provide important insights into a paralog specific function of SUMO1, and suggest that zinc levels could play a crucial role in regulating SUMO1-SIM interactions required for PML-NB formation and function.

Indexed as

Nuclear BodiesPromyelocytic Leukemia ProteinSUMO-1 ProteinZincAmino Acid MotifsTranscription FactorsPromyelocytic Leukemia ProteinSUMO-1 ProteinTranscription FactorsZinc

Identifiers

PMID35871297
PMCPMC9371903
OpenAlexW4286797697

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.