Mitofusins: ubiquitylation promotes fusion

• 来源期刊: 细胞研究（英文版）
• 年，卷（期）: 2014,（4）
• 页码范围: 387-388
• 页数: 2页
• 语种: 英文
• DOI: 10.1038/cr.2014.23

摘要

Mitochondrial genes including Mfn2 are at the center of many diseases,underscoring their potential as a therapeutical target.The Chen group now identified 15-oxospiramilactone as a chemical inhibitor of the mammalian deubiquitylase USP30,acting on Mfn1 and Mfn2. Mitofusins,Fzol in yeast and Mfnl and Mfn2 in mammals,are ubiquitylated and this post-translational modification has both positive and negative consequences on mitochondrial fusion [1].The process of ubiquitylation requires enzymes belonging to three classes of proteins called El,E2 and E3,which catalyze a cascade of successive steps leading to the covalent attachment of the modifier to its target protein [2].Deubiquitylating enzymes render this modification reversible,thus offering further possibilities for regulation [2].