Identification and characterization of modular domains that bind ubiquitin

Michael French*, Kurt Swanson, Susan C. Shih, Ishwar Radhakrishnan, Linda Hicke

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

11 Scopus citations

Abstract

To receive and transmit the information carried by ubiquitin signals, cells have evolved an array of modular ubiquitin-binding domains. These domains bind directly and noncovalently to monoubiquitin and polyubiquitin chains and are found within proteins that function in diverse biological processes. Ubiquitin-binding domains characterized thus far are generally small and structurally diverse, yet they all interact with the same hydrophobic patch on the surface of ubiquitin. The rapid identification and characterization of ubiquitin-binding domains has been accomplished through the extensive use of bioinformatics, biochemistry, molecular biology, and biophysics. Here, we discuss the strategies and tools that have been most successful in the identification and characterization of ubiquitin-binding domains.

Original languageEnglish (US)
Article number9
Pages (from-to)135-157
Number of pages23
JournalMethods in enzymology
Volume399
DOIs
StatePublished - 2005

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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