ArticleScientific reports2016
SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The trial behind it
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Who cites it
12 citing papers in PubMed, 12 citations in OpenAlex.
- PSEN1 mutant marmoset fibroblasts mimic multi-omic signatures of Alzheimer's disease.bioRxiv : the preprint server for biology · 2026Article
- Resurgence of magnetic resonance techniques in the era of AlphaFold.Biophysical reviews · 2025Review
- Chaperone-dependent and chaperone-independent functions of carboxylate clamp tetratricopeptide repeat (CC-TPR) proteins.Trends in biochemical sciences · 2025Review
- USP5 enhances SGTA mediated protein quality control.PloS one · 2022Article
- Exploration of binary protein-protein interactions between tick-borne flaviviruses and Ixodes ricinus.Parasites & vectors · 2021Article
- Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome.Biomolecules · 2020Review
- TPR-containing proteins control protein organization and homeostasis for the endoplasmic reticulum.Critical reviews in biochemistry and molecular biology · 2019Review
- The roles of cytosolic quality control proteins, SGTA and the BAG6 complex, in disease.Advances in protein chemistry and structural biology · 2019Review
- Article
- Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.BMC biology · 2018Article
- Mechanisms of Tail-Anchored Membrane Protein Targeting and Insertion.Annual review of cell and developmental biology · 2017Review
- Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.Frontiers in molecular biosciences · 2017Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.