ArticleJournal of cachexia, sarcopenia and muscle2016
UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes.
Article in Journal of cachexia, sarcopenia and muscle, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
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- From tuberculosis bedside to bench: UBE2B splicing as a potential biomarker and its regulatory mechanism.Signal transduction and targeted therapy · 2023Article
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- MuRF1/TRIM63, Master Regulator of Muscle Mass.International journal of molecular sciences · 2020Review
- Bioinformatics analysis of microRNA linked to ubiquitin proteasome system in traumatic osteonecrosis of the femoral head.Medicine · 2020Observational
- LncRNAs-directed PTEN enzymatic switch governs epithelial-mesenchymal transition.Cell research · 2019Article
- Contemporary publication patterns in the Journal of Cachexia, Sarcopenia and Muscle by type and sub-speciality: facts and numbers.Journal of cachexia, sarcopenia and muscle · 2018Article
- A muscle-specific MuRF1-E2 network requires stabilization of MuRF1-E2 complexes by telethonin, a newly identified substrate.Journal of cachexia, sarcopenia and muscle · 2018Article
- Differentially expressed alternatively spliced genes in skeletal muscle from cancer patients with cachexia.Journal of cachexia, sarcopenia and muscle · 2018Article
- Oodles of opportunities: the Journal of Cachexia, Sarcopenia and Muscle in 2017.Journal of cachexia, sarcopenia and muscle · 2017Article
- UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes.Journal of cachexia, sarcopenia and muscle · 2016Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSkeletal muscle protein loss is an adaptive response to various patho-physiological situations, and the ubiquitin proteasome system (UPS) is responsible for the degradation of the bulk of muscle proteins. The role of E2 ubiquitin-conjugating enzymes is still poorly understood in skeletal muscle.
methodsWe screened for E2s expression levels in C2C12 myotubes submitted to the catabolic glucocorticoid dexamethasone (Dex).
resultsOne micromolar Dex induced an accumulation of proteasome substrates (polyUb conjugates) and an overexpression of the muscle-specific E3 ligase MuRF1 and of six E2 enzymes, UBE2A, UBE2B, UBE2D1, UBE2D2, UBE2G1, and UBE2J1. However, only MuRF1 and UBE2B were sensitive to mild catabolic conditions (0.16 μM Dex). UBE2B knockdown induced a sharp decrease of total (-18%) and K48 (-28%) Ub conjugates, that is, proteasome substrates, indicating an important role of UBE2B in the overall protein breakdown in catabolic myotubes.
conclusionsInterestingly, these results indicate an important role of UBE2B on muscle protein homeostasis during catabolic conditions.
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