Journal ArticleDOI
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
TLDR
Comprehensive understanding of how HSP90 functions promises not only to provide new avenues for therapeutic intervention, but to shed light on fundamental biological questions.Abstract:
Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched in signal transducers, including kinases and transcription factors. Therefore, HSP90 regulates diverse cellular functions and exerts marked effects on normal biology, disease and evolutionary processes. Recent structural and functional analyses have provided new insights on the transcriptional and biochemical regulation of HSP90 and the structural dynamics it uses to act on a diverse client repertoire. Comprehensive understanding of how HSP90 functions promises not only to provide new avenues for therapeutic intervention, but to shed light on fundamental biological questions.read more
Citations
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Journal ArticleDOI
Interplay between HSP90 and Nrf2 pathways in diabetes-associated atherosclerosis
Iolanda Lázaro,Ainhoa Oguiza,Carlota Recio,Laura Lopez-Sanz,Susana Bernal,Jesús Egido,Carmen Gomez-Guerrero +6 more
TL;DR: HSP90 inhibition protects from atherosclerosis in experimental diabetes through the induction of Nrf2-dependent cytoprotective mechanisms, reinforcing its therapeutic potential.
Journal ArticleDOI
Modulation of Human Hsp90α Conformational Dynamics by Allosteric Ligand Interaction at the C-Terminal Domain.
TL;DR: Evidence is found for the selective allosteric activation and inhibition of Hsp90’s conformational transition toward the closed state in response to ligand binding and shed valuable insight to further the understanding of allostero-drug design and Hsp 90‘s complexAllosteric mechanism of action.
Journal ArticleDOI
Comprehensive interactome profiling of the human Hsp70 network highlights functional differentiation of J domains
Benjamin L. Piette,Benjamin L. Piette,Nader Alerasool,Zhen Yuan Lin,Jessica Lacoste,Mandy H. Y. Lam,Wesley Wei Qian,Stephanie Tran,Brett Larsen,Eric I. Campos,Jian Peng,Anne-Claude Gingras,Anne-Claude Gingras,Mikko Taipale +13 more
TL;DR: In this paper, affinity purification-mass spectrometry (AP-MS) and proximity-dependent biotinylation (BioID) were combined to characterize the interactome of all human JDPs and Hsp70s.
Journal ArticleDOI
Molecular Chaperone HSP90 Is Necessary to Prevent Cellular Senescence via Lysosomal Degradation of p14ARF
Su Yeon Han,Andrew H. Ko,Haruhisa Kitano,Chel Hun Choi,Min Sik Lee,Jin-Ho Seo,Junya Fukuoka,Soo-Youl Kim,Stephen M. Hewitt,Joon-Yong Chung,Jaewhan Song +10 more
TL;DR: An unconventional p14ARF degradation pathway induced by the chaperone HSP90 in association with the E3 ubiquitin ligase C-terminus of HSP70-interacting protein (CHIP) is reported, which is correlated with poor prognosis in patients with NSCLC.
Journal ArticleDOI
Mouse cytomegalovirus egress protein pM50 interacts with cellular endophilin-A2
Frederic Lemnitzer,Verena Raschbichler,Dominika Kolodziejczak,Lars Israel,Axel Imhof,Susanne M. Bailer,Ulrich H. Koszinowski,Zsolt Ruzsics +7 more
TL;DR: Recombinant viruses, which express affinity‐tagged pM50 and/or pM53, the pUL34 and pUL31 homologues of the murine cytomegalovirus are generated, and it is found that endophilin‐A2 binds to pM 50 directly, and this interaction seems to be conserved in the p UL34 family.
References
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