Proteomic interrogation of HSP90 and insights for medical research.

Détails

ID Serval
serval:BIB_F42DE0F4D3A4
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Titre
Proteomic interrogation of HSP90 and insights for medical research.
Périodique
Expert review of proteomics
Auteur(s)
Weidenauer L., Wang T., Joshi S., Chiosis G., Quadroni M.R.
ISSN
1744-8387 (Electronic)
ISSN-L
1478-9450
Statut éditorial
Publié
Date de publication
12/2017
Peer-reviewed
Oui
Volume
14
Numéro
12
Pages
1105-1117
Langue
anglais
Notes
Publication types: Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
Publication Status: ppublish
Résumé
Heat shock protein 90 (HSP90) regulates protein homeostasis in eukaryotes. As a 'professional interactor', HSP90 binds to and chaperones many proteins and has both housekeeping and disease-related functions but its regulation remains in part elusive. HSP90 complexes are a target for therapy, notably against cancer, and several inhibitors are currently in clinical trials. Proteomic studies have revealed the vast interaction network of HSP90 and, in doing so, the extent of cellular processes the chaperone takes part in, especially in yeast and human cells. Furthermore, small-molecule inhibitors were used to probe the global impact of its inhibition on the proteome. Areas covered: We review here recent HSP90-related interactomics and total proteome studies and their relevance for research on cancer, neurodegenerative and pathogen diseases. Expert commentary: Proteomics experiments are our best chance to identify the context-dependent global proteome of HSP90 and thus uncover and understand its disease-specific biology. However, understanding the complexity of HSP90 will require multiple complementary, quantitative approaches and novel bioinformatics to translate interactions into ordered functional networks and pathways. Developing therapies will necessitate more knowledge on HSP90 complexes and networks with disease relevance and on total proteome changes induced by their perturbation. Most work has been done in cancer, thus a lot remains to be done in the context of other diseases.
Mots-clé
HSP90 Heat-Shock Proteins/antagonists & inhibitors, HSP90 Heat-Shock Proteins/metabolism, Host-Pathogen Interactions, Humans, Neoplasms/drug therapy, Neoplasms/metabolism, Neurodegenerative Diseases/drug therapy, Neurodegenerative Diseases/metabolism, Protein Processing, Post-Translational, Proteomics/methods, HSP90 interactome, HSP90 networks, cancer, chaperome, chaperones, epichaperome, human disease, proteomics
Pubmed
Web of science
Création de la notice
19/10/2017 9:34
Dernière modification de la notice
05/08/2018 15:26
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