ReviewThe international journal of biochemistry & cell biology2013
Deubiquitinases in skeletal muscle atrophy.
Review in The international journal of biochemistry & cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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.
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Who cites it
18 citing papers in PubMed, 38 citations in OpenAlex.
- Myofibrillar protein accumulation but reduced protein synthesis in PDCD4-depleted myotubes.PloS one · 2026Article
- Transcriptome analysis of muscle atrophy in Leizhou black goats: identification of key genes and insights into limb-girdle muscular dystrophy.BMC genomics · 2025Article
- Deubiquitinases in muscle physiology and disorders.Biochemical Society transactions · 2024Review
- USP18 is an essential regulator of muscle cell differentiation and maturation.Cell death & disease · 2023Article
- Frailty and the Interactions between Skeletal Muscle, Bone, and Adipose Tissue-Impact on Cardiovascular Disease and Possible Therapeutic Measures.International journal of molecular sciences · 2023Review
- Interconnection between Cardiac Cachexia and Heart Failure-Protective Role of Cardiac Obesity.Cells · 2022Review
- USP2 Inhibits Lung Cancer Pathogenesis by Reducing ARID2 Protein Degradation via Ubiquitination.BioMed research international · 2022Article
- Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation.Biomolecules · 2021Review
- Muscle Proteomic and Transcriptomic Profiling of Healthy Aging and Metabolic Syndrome in Men.International journal of molecular sciences · 2021Article
- USP2-Related Cellular Signaling and Consequent Pathophysiological Outcomes.International journal of molecular sciences · 2021Review
- Article
- Gene Co-expression Analysis Indicates Potential Pathways and Regulators of Beef Tenderness in Nellore Cattle.Frontiers in genetics · 2018Article
- Overexpression of ubiquitin specific peptidase 14 predicts unfavorable prognosis in esophageal squamous cell carcinoma.Thoracic cancer · 2017Article
- Effect of the specific proteasome inhibitor bortezomib on cancer-related muscle wasting.Journal of cachexia, sarcopenia and muscle · 2016Article
- Skeletal muscle wasting in cachexia and sarcopenia: molecular pathophysiology and impact of exercise training.Journal of cachexia, sarcopenia and muscle · 2015Review
- Skeletal muscle myotubes in severe obesity exhibit altered ubiquitin-proteasome and autophagic/lysosomal proteolytic flux.Obesity (Silver Spring, Md.) · 2015Article
- Chronically endurance-trained individuals preserve skeletal muscle mitochondrial gene expression with age but differences within age groups remain.Physiological reports · 2014Article
- An ethanolic extract of Artemisia dracunculus L. regulates gene expression of ubiquitin-proteasome system enzymes in skeletal muscle: potential role in the treatment of sarcopenic obesity.Nutrition (Burbank, Los Angeles County, Calif.)Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The ubiquitin proteasome system plays a critical role in skeletal muscle atrophy. A large body of research has revealed that many ubiquitin ligases are induced and play an important role in mediating the wasting. However, relatively little is known about the roles of deubiquitinases in this process. Although it might be expected that deubiquitinases would be downregulated in atrophying muscles to promote ubiquitination and degradation of muscle proteins, this has not to date been demonstrated. Instead several deubiquitinases are induced in atrophying muscle, in particular USP19 and USP14. USP19, USP2 and A20 are also implicated in myogenesis. USP19 has been most studied to date. Its expression is increased in both systemic and disuse forms of atrophy and can be regulated through a p38 MAP kinase signaling pathway. In cultured muscle cells, it decreases the expression of myofibrillar proteins by apparently suppressing their transcription indicating that the ubiquitin proteasome system may be activated in skeletal muscle to not only increase protein degradation, but also to suppress protein synthesis. Deubiquitinases may be upregulated in atrophy in order to maintain the pool of free ubiquitin required for the increased overall conjugation and degradation of muscle proteins as well as to regulate the stability and function of proteins that are essential in mediating the wasting. Although deubiquitinases are not well studied, these early insights indicate that some of these enzymes play important roles and may be therapeutic targets for the prevention and treatment of muscle atrophy. This article is part of a Directed Issue entitled: Molecular basis of muscle wasting.
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Registered trials
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.