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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Thapaliya A,Nyathi Y,Martínez-Lumbreras S,Krysztofinska EM,Evans NJ,Terry IL,High S,Isaacson RLdoi
10.1038/srep36622subject
Has Abstractpub_date
2016-11-09 00:00:00pages
36622issn
2045-2322pii
srep36622journal_volume
6pub_type
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