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Erratum published on 4 December 2018, see Cells 2018, 7(12), 242.

Open AccessFeature PaperArticle
Cells 2018, 7(11), 214; https://doi.org/10.3390/cells7110214

UBE2E1 Is Preferentially Expressed in the Cytoplasm of Slow-Twitch Fibers and Protects Skeletal Muscles from Exacerbated Atrophy upon Dexamethasone Treatment

1
INRA, UMR 1019, Human Nutrition Unit (UNH), 63122 St Genès Champanelle, France
2
Venetian Institute of Molecular Medicine, 35100 Padova, Italy
*
Author to whom correspondence should be addressed.
Received: 24 September 2018 / Revised: 9 November 2018 / Accepted: 13 November 2018 / Published: 16 November 2018
(This article belongs to the Special Issue Ubiquitination in Health and Disease)
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Abstract

Skeletal muscle mass is reduced during many diseases or physiological situations (disuse, aging), which results in decreased strength and increased mortality. Muscle mass is mainly controlled by the ubiquitin-proteasome system (UPS), involving hundreds of ubiquitinating enzymes (E2s and E3s) that target their dedicated substrates for subsequent degradation. We recently demonstrated that MuRF1, an E3 ubiquitin ligase known to bind to sarcomeric proteins (telethonin, α-actin, myosins) during catabolic situations, interacts with 5 different E2 enzymes and that these E2-MuRF1 couples are able to target telethonin, a small sarcomeric protein, for degradation. Amongst the E2s interacting with MuRF1, E2E1 was peculiar as the presence of the substrate was necessary for optimal MuRF1-E2E1 interaction. In this work, we focused on the putative role of E2E1 during skeletal muscle atrophy. We found that E2E1 expression was restricted to type I and type IIA muscle fibers and was not detectable in type IIB fibers. This strongly suggests that E2E1 targets are fiber-specific and may be strongly linked to the contractile and metabolic properties of the skeletal muscle. However, E2E1 knockdown was not sufficient for preserving the protein content in C2C12 myotubes subjected to a catabolic state (dexamethasone treatment), suggesting that E2E1 is not involved in the development of muscle atrophy. By contrast, E2E1 knockdown aggravated the atrophying process in both catabolic C2C12 myotubes and the Tibialis anterior muscle of mice, suggesting that E2E1 has a protective effect on muscle mass. View Full-Text
Keywords: ubiquitin-proteasome system; E2 ubiquitin-conjugating enzymes; E3 ubiquitin ligases; UBE2E1; MuRF1; skeletal muscle; atrophy; actin; myosin heavy chain ubiquitin-proteasome system; E2 ubiquitin-conjugating enzymes; E3 ubiquitin ligases; UBE2E1; MuRF1; skeletal muscle; atrophy; actin; myosin heavy chain
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Polge, C.; Aniort, J.; Armani, A.; Claustre, A.; Coudy-Gandilhon, C.; Tournebize, C.; Deval, C.; Combaret, L.; Béchet, D.; Sandri, M.; Attaix, D.; Taillandier, D. UBE2E1 Is Preferentially Expressed in the Cytoplasm of Slow-Twitch Fibers and Protects Skeletal Muscles from Exacerbated Atrophy upon Dexamethasone Treatment. Cells 2018, 7, 214.

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