Evidence map›Paper›PMID 28130202›Full record

ReviewBiochimica et biophysica acta. Molecular basis of disease2017

Sub-cellular localization specific SUMOylation in the heart.

Nhat-Tu Le, James F Martin, Keigi Fujiwara, Jun-Ichi Abe

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular basis of disease, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. SUMOylation of TEAD1 Modulates the Mechanism of Pathological Cardiac Hypertrophy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  7. Cardioprotective Strategies After Ischemia-Reperfusion Injury.American journal of cardiovascular drugs : drugs, devices, and other interventions · 2024
    Review
  8. Review
  9. SUMOylation targeting mitophagy in cardiovascular diseases.Journal of molecular medicine (Berlin, Germany) · 2022
    Review
  10. Review
  11. Article
  12. SUMOylation as a Therapeutic Target for Myocardial Infarction.Frontiers in cardiovascular medicine · 2021
    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

4 authors at 2 institutions in 1 country.

Nhat-Tu LeDepartment of Cardiology - Research, Division of Internal Medicine, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.
James F MartinDepartment of Molecular Physiology and Biophysics, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Keigi FujiwaraDepartment of Cardiology - Research, Division of Internal Medicine, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.
Jun-Ichi AbeDepartment of Cardiology - Research, Division of Internal Medicine, The University of Texas MD Anderson Cancer Center, Houston, TX, USA. Electronic address: jabe@mdanderson.org.
The University of Texas MD Anderson Cancer Center · USBaylor College of Medicine · US

Funding

PAR 13-233 cART accelerates vascular aging in HIV infected subjectsR01HL123346 · NHLBI · UNIVERSITY OF ROCHESTER · PI ABE, JUN-ICHI, MAGGIRWAR, SANJAY B. · 2014 to 2018
$3.7M
Disturbed flow-induced TERF2IP post-translational modifications and atherosclerosis.R01HL130193 · NHLBI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI ABE, JUN-ICHI · 2016 to 2019
$2.0M
p90RSK-ERK5 module, efferocytosis, and vulnerable plaque formationR01HL118462 · NHLBI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI ABE, JUN-ICHI · 2014 to 2018
$2.0M
Ubiquitin-like protein modification in diabetic cardiomyopathyR01HL108551 · NHLBI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI ABE, JUN-ICHI, YANG, JAY · 2011 to 2014
$1.6M
NHLBI NIH HHS R01 HL108551NHLBI NIH HHS R01 HL118462NHLBI NIH HHS R01 HL123346NHLBI NIH HHS R01 HL130193
6 · The paper itself

Abstract

Although the majority of SUMO substrates are localized in the nucleus, SUMOylation is not limited to nuclear proteins and can be also detected in extra-nuclear proteins. In this review, we will highlight and discuss how SUMOylation in different cellular compartments regulate biological processes. First, we will discuss the key role of SUMOylation of proteins in the extra-nuclear compartment in cardiomyocytes, which is overwhelmingly cardio-protective. On the other hand, SUMOylation of nuclear proteins is generally detrimental to the cardiac function mainly because of the trans-repressive nature of SUMOylation on many transcription factors. We will also discuss the potential role of SUMOylation in epigenetic regulation. In this review, we will propose a new concept that shuttling of SUMO proteases between the nuclear and extra-nuclear compartments without changing their enzymatic activity regulates the extent of SUMOylation in these compartments and determines the response and fate of cardiomyocytes after cardiac insults. Approaches focused specifically to inhibit this shuttling in cardiomyocytes will be necessary to understand the whole picture of SUMOylation and its pathophysiological consequences in the heart, especially after cardiac insults. This article is part of a Special Issue entitled: Genetic and epigenetic control of heart failure - edited by Jun Ren & Megan Yingmei Zhang.

Indexed as

SumoylationAnimalsHeart DiseasesHumansMuscle ProteinsMyocardiumMyocytes, CardiacMuscle ProteinsAMPKDRP-1ERK5HDACsNEMOp90RSKPKCαPotassium channelPPARsSENP2SERCA2aSUMOylationUbc9XBP-1

Identifiers

PMID28130202
PMCPMC5716640
OpenAlexW2582327875

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.