Comprehensive identification of substrates for f-box proteins by differential proteomics analysis

Kanae Yumimoto, Masaki Matsumoto, Koji Oyamada, Toshiro Moroishi, Keiichi Nakayama

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

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 Fbxw7α, 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.

Original languageEnglish
Pages (from-to)3175-3185
Number of pages11
JournalJournal of Proteome Research
Volume11
Issue number6
DOIs
Publication statusPublished - Jun 1 2012

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Ubiquitination
Ligases
Ubiquitin
Proteomics
Substrates
Enzymes
F-Box Proteins
Proteins
Screening

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Chemistry(all)

Cite this

Comprehensive identification of substrates for f-box proteins by differential proteomics analysis. / Yumimoto, Kanae; Matsumoto, Masaki; Oyamada, Koji; Moroishi, Toshiro; Nakayama, Keiichi.

In: Journal of Proteome Research, Vol. 11, No. 6, 01.06.2012, p. 3175-3185.

Research output: Contribution to journalArticle

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