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Published on Sep 13, 2012
For more info, visit http://www.bio-rad.com/yt/1/proteonxpr36 Ubiquitin is an important regulatory protein found in almost all eukaryote tissue. Ubiqutin modification of proteins targets them for proteasomal degradation. It also serves many non-proteasomal functions in signal transduction, endocytic trafficking and DNA repair, among others. The functional outcome of ubiquitin modification is dependent upon non-covalent interactions with ubiquitin-binding domains (UBDs). As many as 22 UBDs have been described and it is possible that other UBDs exist but this remains to be determined. Here, Prof. Adriano Marchese reports an important novel UBD that shows a preference for polyubiquitin chains versus mono-ubiquitin. This finding may have significant impact for diseases where cell signaling is perturbed, such as cancer. Surface plasmon resonance (SPR) was used to characterize these interactions.
Presenter: Adriano Marchese, PhD Associate Professor, Pharmacology Loyola University
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