The Ball and Chain of Polyubiquitin Structures

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• 作者：Caterina Alfano¹ ; Serena Faggiano² ; Annalisa Pastore¹ ; ^{annalisa.pastore@crick.ac.uk" class="auth_mail" title="E-mail the corresponding author}
• 关键词：biophysics ; post-translational modifications ; proteasomal pathway ; signalling ; structure ; ubiquitin
• 刊名：Trends in Biochemical Sciences
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：41
• 期：4
• 页码：371-385
• 全文大小：3530 K

文摘

Ubiquitylation is a post-translational modification implicated in several different cellular pathways. The possibility of forming chains through covalent crosslinking between any of the seven lysines, or the initial methionine, and the C terminus of another moiety provides ubiquitin (Ub) with special flexibility in its function in signalling. Here, we review the knowledge accumulated over the past several years about the functions and structural features of polyUb chains. This analysis reveals the need to understand further the functional role of some of the linkages and the structural code that determines recognition of polyUbs by protein partners.