Journal
JOURNAL OF PROTEOME RESEARCH
Volume 11, Issue 6, Pages 3175-3185Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr201216u
Keywords
ubiquitin ligase; F-box protein; substrate identification; differential proteomics
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
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Although elucidation of enzyme substrate relations is fundamental to the advancement of biology, universal approaches to the identification of substrates for a given enzyme have not been established. It is especially difficult to identify substrates for ubiquitin ligases, given that most such substrates are immediately ubiquitylated and degraded as a result of their association with the enzyme. We here describe the development of a new approach, DiPIUS (differential proteomics-based identification of ubiquitylation substrates), to the discovery of substrates for ubiquitin ligases. We applied DiPIUS to Fbxw7 alpha, Skp2, and Fbxl5, three of the most well-characterized F-box proteins, and identified candidate substrates including previously known targets. DiPIUS is thus a powerful tool for unbiased and comprehensive screening for substrates of ubiquitin ligases.
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