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Structural and functional insights into the E3 ligase, RNF126
RNF126 is an E3 ubiquitin ligase that collaborates with the BAG6 sortase complex to ubiquitinate hydrophobic substrates in the cytoplasm that are destined for proteasomal recycling. Composed of a trimeric complex of BAG6, TRC35 and UBL4A the BAG6 sortase is also associated with SGTA, a co-chaperone...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4872217/ https://www.ncbi.nlm.nih.gov/pubmed/27193484 http://dx.doi.org/10.1038/srep26433 |
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author | Krysztofinska, Ewelina M. Martínez-Lumbreras, Santiago Thapaliya, Arjun Evans, Nicola J. High, Stephen Isaacson, Rivka L. |
author_facet | Krysztofinska, Ewelina M. Martínez-Lumbreras, Santiago Thapaliya, Arjun Evans, Nicola J. High, Stephen Isaacson, Rivka L. |
author_sort | Krysztofinska, Ewelina M. |
collection | PubMed |
description | RNF126 is an E3 ubiquitin ligase that collaborates with the BAG6 sortase complex to ubiquitinate hydrophobic substrates in the cytoplasm that are destined for proteasomal recycling. Composed of a trimeric complex of BAG6, TRC35 and UBL4A the BAG6 sortase is also associated with SGTA, a co-chaperone from which it can obtain hydrophobic substrates. Here we solve the solution structure of the RNF126 zinc finger domain in complex with the BAG6 UBL domain. We also characterise an interaction between RNF126 and UBL4A and analyse the competition between SGTA and RNF126 for the N-terminal BAG6 binding site. This work sheds light on the sorting mechanism of the BAG6 complex and its accessory proteins which, together, decide the fate of stray hydrophobic proteins in the aqueous cytoplasm. |
format | Online Article Text |
id | pubmed-4872217 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-48722172016-06-01 Structural and functional insights into the E3 ligase, RNF126 Krysztofinska, Ewelina M. Martínez-Lumbreras, Santiago Thapaliya, Arjun Evans, Nicola J. High, Stephen Isaacson, Rivka L. Sci Rep Article RNF126 is an E3 ubiquitin ligase that collaborates with the BAG6 sortase complex to ubiquitinate hydrophobic substrates in the cytoplasm that are destined for proteasomal recycling. Composed of a trimeric complex of BAG6, TRC35 and UBL4A the BAG6 sortase is also associated with SGTA, a co-chaperone from which it can obtain hydrophobic substrates. Here we solve the solution structure of the RNF126 zinc finger domain in complex with the BAG6 UBL domain. We also characterise an interaction between RNF126 and UBL4A and analyse the competition between SGTA and RNF126 for the N-terminal BAG6 binding site. This work sheds light on the sorting mechanism of the BAG6 complex and its accessory proteins which, together, decide the fate of stray hydrophobic proteins in the aqueous cytoplasm. Nature Publishing Group 2016-05-19 /pmc/articles/PMC4872217/ /pubmed/27193484 http://dx.doi.org/10.1038/srep26433 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ 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/ |
spellingShingle | Article Krysztofinska, Ewelina M. Martínez-Lumbreras, Santiago Thapaliya, Arjun Evans, Nicola J. High, Stephen Isaacson, Rivka L. Structural and functional insights into the E3 ligase, RNF126 |
title | Structural and functional insights into the E3 ligase, RNF126 |
title_full | Structural and functional insights into the E3 ligase, RNF126 |
title_fullStr | Structural and functional insights into the E3 ligase, RNF126 |
title_full_unstemmed | Structural and functional insights into the E3 ligase, RNF126 |
title_short | Structural and functional insights into the E3 ligase, RNF126 |
title_sort | structural and functional insights into the e3 ligase, rnf126 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4872217/ https://www.ncbi.nlm.nih.gov/pubmed/27193484 http://dx.doi.org/10.1038/srep26433 |
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