How do our cells build their protein interactome?
Abstract 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...
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Nature Portfolio
2018
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oai:doaj.org-article:f97f4fd0ce644bb78fe9541ee2c939012021-12-02T15:34:49ZHow do our cells build their protein interactome?10.1038/s41467-018-05448-22041-1723https://doaj.org/article/f97f4fd0ce644bb78fe9541ee2c939012018-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05448-2https://doaj.org/toc/2041-1723Abstract 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.Benoit CoulombePhilippe CloutierMarie-Soleil GauthierNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-3 (2018) |
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Science Q Benoit Coulombe Philippe Cloutier Marie-Soleil Gauthier How do our cells build their protein interactome? |
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Abstract 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 |
article |
author |
Benoit Coulombe Philippe Cloutier Marie-Soleil Gauthier |
author_facet |
Benoit Coulombe Philippe Cloutier Marie-Soleil Gauthier |
author_sort |
Benoit Coulombe |
title |
How do our cells build their protein interactome? |
title_short |
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_sort |
how do our cells build their protein interactome? |
publisher |
Nature Portfolio |
publishDate |
2018 |
url |
https://doaj.org/article/f97f4fd0ce644bb78fe9541ee2c93901 |
work_keys_str_mv |
AT benoitcoulombe howdoourcellsbuildtheirproteininteractome AT philippecloutier howdoourcellsbuildtheirproteininteractome AT mariesoleilgauthier howdoourcellsbuildtheirproteininteractome |
_version_ |
1718386756148002816 |