Ubc9 expression is essential for myotube formation in C2C12.

Experimental Cell Research
Cecilia RiquelmeXuedong Liu

Abstract

Myogenic differentiation is a fundamental biological process that involves a hierarchical series of events that ultimately leads to muscle-specific gene expression and myofiber formation. Posttranslational modifications of the myogenic regulatory factors have been implicated as important regulatory mechanisms in this process. Here we investigate whether covalent protein modification by a small ubiquitin-like modifier (SUMO) that is known to affect transcription factor activity can impact muscle differentiation. We show that the overall load of sumoylated proteins present in myoblasts diminishes progressively throughout myogenesis. Interestingly, knockdown of the SUMO-conjugating enzyme, Ubc9, severely compromises C2C12 muscle cell terminal differentiation. However, it does not affect the expression, the localization and the activation of MyoD and myogenin. These novel results suggest that protein sumoylation plays a pivotal role in myoblast differentiation and is required to regulate the activity of key targets downstream of MyoD and myogenin.

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Citations

Nov 15, 2006·Molecular and Cellular Biology·Jun WangRobert J Schwartz
Dec 14, 2006·Journal of Cell Science·Adeline F DeyrieuxVan G Wilson
Jun 25, 2008·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·Daniel L YamamotoTore Bengtsson
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Mar 15, 2019·Cell Death & Disease·Shruti SrinivasanReshma Taneja
Aug 22, 2020·Experimental Cell Research·Xiuxiu LiuStefano Gastaldello

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