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SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism

Thapaliya, A.
; 
Nyathi, Yvonne
; 
Martínez-Lumbreras, S.
; 
Krysztofinska, E.M.
; 
Evans, N.J.
; 
Terry, I.L.
; 
High, S.
; 
Isaacson, R.L.
Publication Date
2016-11
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Keywords
SGTA, Diverse binding partners, Proteasomal ubiquitin receptor Rpn13, Carboxylate clamp mechanism
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© The Author(s) 2016. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
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openAccess
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2016-10-18
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Life Sciences Publications
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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.
URI
http://hdl.handle.net/10454/17893
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Published version
Citation
Thapaliya A, Nyathi Y, Martínez-Lumbreras S et al (2016) SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism. Scientific Reports. 6: 36622.
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https://doi.org/10.1038/srep36622
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Article
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