Wolberger Cynthia
Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205.
Protein Sci. 2014 Apr;23(4):344-53. doi: 10.1002/pro.2415. Epub 2014 Feb 12.
Ubiquitination is a reversible post-translational modification that plays a dynamic role in regulating most eukaryotic processes. Deubiquitinating enzymes (DUBs), which hydrolyze the isopeptide or peptide linkages joining ubiquitin to substrate lysines or N-termini, therefore play a key role in ubiquitin signaling. Cells employ multiple mechanisms to regulate DUB activity and thus ensure the appropriate biological response. Recent structural studies have shed light on several different mechanisms by which DUB activity and specificity is regulated.
泛素化是一种可逆的翻译后修饰,在调节大多数真核生物过程中发挥动态作用。去泛素化酶(DUBs)可水解连接泛素与底物赖氨酸或N端的异肽键或肽键,因此在泛素信号传导中起关键作用。细胞采用多种机制来调节DUB活性,从而确保适当的生物学反应。最近的结构研究揭示了几种调节DUB活性和特异性的不同机制。