Evidence map›Paper›PMID 15601779›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I.

Vishram Kedar, Holly McDonough, Ranjana Arya, Hui-Hua Li, Howard A Rockman, Cam Patterson

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 164 papers.

0numbers the graph read from it
0cells of the map it votes in
164citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

164 citing papers in PubMed, 328 citations in OpenAlex.

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  9. Review
  10. The role of mechanosignaling in the control of myocardial mass.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Targeting MuRF1 to Combat Skeletal Muscle Wasting in Cardiac Cachexia: Mechanisms and Therapeutic Prospects.Medical science monitor : international medical journal of experimental and clinical research · 2024
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Secreted Protein Acidic and Rich in Cysteine (Diseases (Basel, Switzerland) · 2023
    Article

104 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

Vishram KedarCarolina Cardiovascular Biology Center, University of North Carolina, Chapel Hill, NC 27599-7126, USA.
Holly McDonough
Ranjana Arya
Hui-Hua Li
Howard A Rockman
Cam Patterson
Duke University · USCardiovascular Research Center · BR

Funding

MECHANISMS OF MALADAPTATION IN HEART FAILURER01HL056687 · NHLBI · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI Howard A Rockman · 1996 to 2026
$12.3M
Myocyte Signaling and the Response to StressR37HL065619 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PATTERSON, WINSTON C · 2010 to 2019
$3.7M
CHIP: A link between the chaperone &proteasome systemsR01GM061728 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SCHISLER, JONATHAN C. · 2001 to 2013
$3.4M
Myocyte signaling and the response to stressR01HL065619 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PATTERSON, WINSTON C · 2001 to 2009
$2.7M
NHLBI NIH HHS HL56687NHLBI NIH HHS HL65619NHLBI NIH HHS R01 HL056687NHLBI NIH HHS R01 HL065619NHLBI NIH HHS R37 HL065619NIGMS NIH HHS GM61728NIGMS NIH HHS R01 GM061728
6 · The paper itself

Abstract

Muscle-specific RING finger protein 1 (MuRF1) is a sarcomere-associated protein that is restricted to cardiac and skeletal muscle. In skeletal muscle, MuRF1 is up-regulated by conditions that provoke atrophy, but its function in the heart is not known. The presence of a RING finger in MuRF1 raises the possibility that it is a component of the ubiquitin-proteasome system of protein degradation. We performed a yeast two-hybrid screen to search for interaction partners of MuRF1 in the heart that might be targets of its putative ubiquitin ligase activity. This screen identified troponin I as a MuRF1 partner protein. MuRF1 and troponin I were found to associate both in vitro and in vivo in cultured cardiomyocytes. MuRF1 reduced steady-state troponin I levels when coexpressed in COS-7 cells and increased degradation of endogenous troponin I protein in cardiomyocytes. The degradation of troponin I in cardiomyocytes was associated with the accumulation of ubiquitylated intermediates of troponin I and was proteasome-dependent. In vitro, MuRF1 functioned as a ubiquitin ligase to catalyze ubiquitylation of troponin I through a RING finger-dependent mechanism. In isolated cardiomyocytes, MuRF1 reduced indices of contractility. In cardiomyocytes, these processes may determine the balance between hypertrophic and antihypertrophic signals and the regulation of myocyte contractile responses in the setting of heart failure.

Indexed as

AnimalsAnimals, NewbornAtrophyCatalysisCells, CulturedCOS CellsFluorescent Antibody Technique, IndirectGene LibraryGreen Fluorescent ProteinsHeartHeart VentriclesHumansHypertrophyMuscle ProteinsMyocardiumPlasmidsGreen Fluorescent ProteinsMuscle ProteinsProteasome Endopeptidase ComplexTRIM63 protein, humanTrim63 protein, ratTripartite Motif ProteinsTroponin IUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID15601779
PMCPMC539735
OpenAlexW1992427679

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.