Apr 25, 2006

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.

Mentioned in this Paper

SUMO1 gene
Myoblasts
Cell Cycle Progression
Establishment and Maintenance of Localization
Antigens, Differentiation
MYOG wt Allele
Biochemical Pathway
MYOD1 gene
Transcription Factor Activity [MoA]
Covalent Interaction

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