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• W2549125891 abstract "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." @default.
• W2549125891 created "2016-11-30" @default.
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• W2549125891 date "2016-11-09" @default.
• W2549125891 modified "2023-09-26" @default.
• W2549125891 title "SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism" @default.
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• W2549125891 doi "https://doi.org/10.1038/srep36622" @default.
• W2549125891 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5101480" @default.
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