摘要
泛素化(Ubiquitylation)是目前真核细胞内已知的最复杂的翻译后修饰。泛素化底物的识别需要一类特异性受体蛋白介导,这些受体蛋白往往包含一个或多个泛素结合结构域(UBDs)。UBD-泛素间的特异性结合决定了泛素化底物功能的特异性。目前已发现20多种UBDs超家族可识别泛素化底物上的特异性功能团进而传递信号。因此深入了解UBD的识别机制对新UBD的发现及泛素化底物的鉴定具有重要意义。
Ubiquitylation is the most complex post-translational modification in eukaryotes.The cellular processes modulated by ubiquitylation are deciphered by a specific ubiquitylated target by a'downstream'ubiquitin receptor,which is also known as a ubiquitin-binding protein(UBP),containing a class of specific ubiquitin binding domains(UBD).The fate or function of ubiquitylated target was determined by this specific UBD-ubiquitin interactions.Over twenty distinct ubiquitin-binding domain(UBD)families specifically recognize the motif one the ubiquitylated target surfaces.Therefore,it is of great significance to deeply understand the regulatory mechanisms of UBDubiquitin interactions for found out the new UBD and the deep mining of ubiquitinated proteome(ubiquitome).
作者
王京伟
武军驻
WANG Jing-wei WU Jun-zhu(Department of Clinic Laboratory, Renmin Hospital of Wuhan University, Wuhan 430060, Chi na Department of Biochemistry, School of Medicine, Wuhan University, Wuhan 430071, China)
出处
《微循环学杂志》
2017年第3期73-79,共7页
Chinese Journal of Microcirculation
基金
武汉大学青年教师自主科研项目(2042015kf0113)