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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Unusual roles of host metabolic enzymes and housekeeping proteins in plant virus replication.
TL;DR: This review compares the newly discovered roles of selected metabolic enzymes and housekeeping proteins in plant (+)RNA virus replication with their original cellular functions and the different consequences when utilized by different viruses.
Journal ArticleDOI
Spermatogenesis arrest caused by conditional deletion of Hsp90α in adult mice
Chiaki Kajiwara,Shiho Kondo,Shizuha Uda,Lei Dai,Tomoko Ichiyanagi,Tomoki Chiba,Satoshi Ishido,Takehiko Koji,Heiichiro Udono +8 more
TL;DR: The results suggest that the AR, specifically chaperoned by Hsp90&agr; in spermatogonia, is critical for maintenance of established sperMatogenesis and for survival of sper matocytes in adult testis, in addition to setting the first wave of s permatogenesis before puberty.
Journal ArticleDOI
Adaptive variability to low‐pH river discharges in Acartia tonsa and stress responses to high PCO2 conditions
Victor M. Aguilera,Victor M. Aguilera,Cristian A. Vargas,Marco A. Lardies,Marco A. Lardies,María Josefina Poupin +5 more
TL;DR: Adaptation to local fluctuations in seawater pH seems to play a significant role in the response of planktonic populations to OA-associated conditions, and expression of both the Hsp70 and Ferritin genes in coastal copepods was significantly higher after acclimation to high PCO2 conditions.
Journal ArticleDOI
DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA
TL;DR: The results indicate that CYT-19 functions predominantly by disrupting accessible RNA secondary structure and depends on spontaneous openings in tightly packed RNAs to gain access to RNA helices, which could bias DEAD-box proteins to act on misfolded RNAs and ribonucleoproteins, which are likely to be less compact and more dynamic than their native counterparts.
Journal ArticleDOI
Both the charged linker region and ATPase domain of Hsp90 are essential for Rad51-dependent DNA repair.
Tanvi Suhane,Shyamasree Laskar,Siddheshwari Advani,Nabamita Roy,Shalu M. Varunan,Dibyendu Bhattacharyya,Sunanda Bhattacharyya,Mrinal Kanti Bhattacharyya +7 more
TL;DR: The results show that the Hsp82 chaperone, the ortholog of mammalian Hsp90, is indispensable for homologous-recombination (HR)-mediated DNA repair in the budding yeast Saccharomyces cerevisiae.
References
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Journal ArticleDOI
Mechanism of Activation of the Raf-Erk Signaling Pathway by Oncogenic Mutations of B-Raf
Paul T C Wan,Mathew J. Garnett,S. Mark Roe,Sharlene Lee,Dan Niculescu-Duvaz,Valerie M. Good,Cancer Genome,C. Michael Jones,Christopher J. Marshall,Caroline J. Springer,David Barford,Richard Marais +11 more
TL;DR: The high activity mutants signal to ERK by directly phosphorylating MEK, whereas the impaired activity mutants stimulate MEK by activating endogenous C-RAF, possibly via an allosteric or transphosphorylation mechanism.
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HSP90 and the chaperoning of cancer.
TL;DR: Pharmacologically 'bribing' the essential guard duty of the chaperone HSP90 (heat-shock protein of 90 kDa) seems to offer a unique anticancer strategy of considerable promise.
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Hsp90 as a capacitor for morphological evolution
TL;DR: It is reported that when Drosophila Hsp90 is mutant or pharmacologically impaired, phenotypic variation affecting nearly any adult structure is produced, with specific variants depending on the genetic background and occurring both in laboratory strains and in wild populations.
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Adapting proteostasis for disease intervention.
TL;DR: The proteostasis network is described, a set of interacting activities that maintain the health of proteome and the organism that has the potential to ameliorate some of the most challenging diseases of this era.
Journal ArticleDOI
Function and regulation of cullin-RING ubiquitin ligases.
TL;DR: This review focuses on the composition, regulation and function of cullin–RING ligases, and describes how these enzymes can be characterized by a set of general principles.