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The E3 Ubiquitin Ligase CHIP and the Molecular Chaperone Hsc70 Form a Dynamic, Tethered Complex

Smith M, et al., 52(32), 5354-64, Biochemistry, 2013

The E3 ubiquitin ligase CHIP (C-terminus of Hsc70 Interacting Protein) binds to the molecular chaperone Hsc70, and this complex is important in both the ubiquitination of Hsc70 and the turnover of Hsc70-bound clients. In this study, the authors characterized the binding of Hsc70 to CHIP using the Octet RED96 system, fluorescence polarization, and NMR spectroscopy. For the Octet experiments, Hsc70 proteins and the C-terminal peptide were biotinylated and loaded onto Streptavidin biosensors.

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