SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism
| Autor: | Santiago Martínez-Lumbreras, Isabelle L. Terry, Nicola J. Evans, Rivka L. Isaacson, Arjun Thapaliya, Ewelina M. Krysztofinska, Yvonne Nyathi, Stephen High |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Multidisciplinary Membrane Glycoproteins Protein domain Intracellular Signaling Peptides and Proteins Context (language use) Plasma protein binding Biology Article Cell biology 03 medical and health sciences Tetratricopeptide Cytosol 030104 developmental biology Ubiquitin Proteasome Membrane protein Protein Domains C700 Molecular Biology Biophysics and Biochemistry biology.protein Humans Carrier Proteins Molecular Chaperones Protein Binding |
| Zdroj: | Thapaliya, A, Nyathi, Y, Martinez Lumbreras, S, Krysztofinska, E, Evans, N, Terry, I L, High, S & Isaacson, R L 2016, ' SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism ', Scientific Reports, vol. 6, 36622 . https://doi.org/10.1038/srep36622 Scientific Reports |
| Popis: | The fate of secretory and membrane proteins that mislocalize to the cytosol is decided by a collaboration between cochaperone SGTA (small, glutamine-rich, tetratricopeptide repeat protein alpha) and the BAG6 complex, whose operation relies on multiple transient and subtly discriminated interactions with diverse binding partners. These include chaperones, membrane-targeting proteins and ubiquitination enzymes. Recently a direct interaction was discovered between SGTA and the proteasome, mediated by the intrinsic proteasomal ubiquitin receptor Rpn13. Here, we structurally and biophysically characterize this binding and identify a region of the Rpn13 C-terminal domain that is necessary and sufficient to facilitate it. We show that the contact occurs through a carboxylate clamp-mediated molecular recognition event with the TPR domain of SGTA, and provide evidence that the interaction can mediate the association of Rpn13 and SGTA in a cellular context. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|