期刊
CELL DEATH AND DIFFERENTIATION
卷 16, 期 6, 页码 921-932出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/cdd.2009.27
关键词
ubiquitin-proteasome system; ASB2; muscle differentiation; filamin
资金
- Centre National de la Recherche Scientifique (CNRS)
- Universite de Toulouse, the Universite Pierre et Marie Curie
- National Institutes of Health [GM068600, HL089433]
- Universite Paul Sabatier
- Agence Nationale de la Recherche
- Association Francaise contre les Myopathies
- Association pour la Recherche sur le Cancer
- Fondation pour la Recherche Medicale
Ubiquitin-mediated protein degradation is the main mechanism for controlled proteolysis, which is crucial for muscle development and maintenance. The ankyrin repeat-containing protein with a suppressor of cytokine signaling box 2 gene (ASB2) encodes the specificity subunit of an E3 ubiquitin ligase complex involved in differentiation of hematopoietic cells. Here, we provide the first evidence that a novel ASB2 isoform, ASB2 beta, is important for muscle differentiation. ASB2 beta is expressed in muscle cells during embryogenesis and in adult tissues. ASB2 beta is part of an active E3 ubiquitin ligase complex and targets the actin-binding protein filamin B (FLNb) for proteasomal degradation. Thus, ASB2 beta regulates FLNb functions by controlling its degradation. Knockdown of endogenous ASB2 beta by shRNAs during induced differentiation of C2C12 cells delayed FLNb degradation as well as myoblast fusion and expression of muscle contractile proteins. Finally, knockdown of FLNb in ASB2 beta knockdown cells restores myogenic differentiation. Altogether, our results suggest that ASB2 beta is involved in muscle differentiation through the targeting of FLNb to destruction by the proteasome. Cell Death and Differentiation (2009) 16, 921-932; doi: 10.1038/cdd.2009.27; published online 20 March 2009
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