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- W2060996957 abstract "Essential cellular processes, such as cell division, rely on the coordinated destruction of proteins. The predominant means of accomplishing this involves a large cellular machine, the proteasome ( 1 ). Proteasomal degradation ensues when proteins are modified with ubiquitin, a small protein, that has many different roles ( 2 ). This tagging involves a carrier protein (an E2 ubiquitin-conjugating enzyme) and a substrate-determining protein (an E3 ligase). For example, during the cell division cycle, a large multiprotein E3 ligase, the anaphase-promoting complex/cyclosome (APC/C), utilizes two E2 enzymes, UBE2C and UBE2S, to target proteins for destruction ( 3 ). On pages 199 and 200 of this issue, two Research Articles by Lu et al. focus on these reactions and illuminate, at the single-molecule level, the process of ubiquitination by APC/C ( 4 ), as well as the recognition and subsequent destruction of APC/C substrates by proteasomes ( 5 ). Both studies substantially enrich our knowledge of ubiquitination and degradation, reveal new properties of APC/C and the proteasome, and challenge established concepts about the ubiquitin-proteasome system." @default.
- W2060996957 created "2016-06-24" @default.
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- W2060996957 date "2015-04-09" @default.
- W2060996957 modified "2023-09-25" @default.
- W2060996957 title "Details of destruction, one molecule at a time" @default.
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- W2060996957 doi "https://doi.org/10.1126/science.aab0931" @default.
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