Cargando…

How do our cells build their protein interactome?

Chaperones are cellular factors that help in the folding of newly synthesized polypeptides (or clients) and, in some cases, ensure their integration within larger complexes. They often require non-client proteins, or co-chaperones, to help drive specificity to particular target polypeptides or facil...

Descripción completa

Detalles Bibliográficos
Autores principales: Coulombe, Benoit, Cloutier, Philippe, Gauthier, Marie-Soleil
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6063932/
https://www.ncbi.nlm.nih.gov/pubmed/30054485
http://dx.doi.org/10.1038/s41467-018-05448-2
_version_ 1783342625689960448
author Coulombe, Benoit
Cloutier, Philippe
Gauthier, Marie-Soleil
author_facet Coulombe, Benoit
Cloutier, Philippe
Gauthier, Marie-Soleil
author_sort Coulombe, Benoit
collection PubMed
description Chaperones are cellular factors that help in the folding of newly synthesized polypeptides (or clients) and, in some cases, ensure their integration within larger complexes. They often require non-client proteins, or co-chaperones, to help drive specificity to particular target polypeptides or facilitate the nucleotide hydrolysis cycle of some chaperones. The latest findings on the characterization of the PAQosome (Particle for Arrangement of Quaternary structure; formerly known as R2TP/PFDL complex) published recently in Nature Communications help to explain how this particular co-chaperone plays a central role in organizing our proteome into protein complexes and networks. The exploitation by the cell of alternative PAQosomes formed through the differential integration of homologous subunits, in conjunction with the use of several adaptors (specificity factors), provide the conceptual basis for interaction of multiple clients in a structure that is favorable to their simultaneous binding en route to protein complex and network assembly/maturation.
format Online
Article
Text
id pubmed-6063932
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-60639322018-07-30 How do our cells build their protein interactome? Coulombe, Benoit Cloutier, Philippe Gauthier, Marie-Soleil Nat Commun Comment Chaperones are cellular factors that help in the folding of newly synthesized polypeptides (or clients) and, in some cases, ensure their integration within larger complexes. They often require non-client proteins, or co-chaperones, to help drive specificity to particular target polypeptides or facilitate the nucleotide hydrolysis cycle of some chaperones. The latest findings on the characterization of the PAQosome (Particle for Arrangement of Quaternary structure; formerly known as R2TP/PFDL complex) published recently in Nature Communications help to explain how this particular co-chaperone plays a central role in organizing our proteome into protein complexes and networks. The exploitation by the cell of alternative PAQosomes formed through the differential integration of homologous subunits, in conjunction with the use of several adaptors (specificity factors), provide the conceptual basis for interaction of multiple clients in a structure that is favorable to their simultaneous binding en route to protein complex and network assembly/maturation. Nature Publishing Group UK 2018-07-27 /pmc/articles/PMC6063932/ /pubmed/30054485 http://dx.doi.org/10.1038/s41467-018-05448-2 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Comment
Coulombe, Benoit
Cloutier, Philippe
Gauthier, Marie-Soleil
How do our cells build their protein interactome?
title How do our cells build their protein interactome?
title_full How do our cells build their protein interactome?
title_fullStr How do our cells build their protein interactome?
title_full_unstemmed How do our cells build their protein interactome?
title_short How do our cells build their protein interactome?
title_sort how do our cells build their protein interactome?
topic Comment
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6063932/
https://www.ncbi.nlm.nih.gov/pubmed/30054485
http://dx.doi.org/10.1038/s41467-018-05448-2
work_keys_str_mv AT coulombebenoit howdoourcellsbuildtheirproteininteractome
AT cloutierphilippe howdoourcellsbuildtheirproteininteractome
AT gauthiermariesoleil howdoourcellsbuildtheirproteininteractome