HSP90


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HSP90

A generic term for a family of molecular chaperones which play a key role in protein folding and quality control for a range of client proteins. Functional HSP90s operate as dimers, have intrinsic ATPase activity, act in concert with other chaperones (e.g., HSP70) and are regulated by co-chaperones/accessory proteins (e.g., HOP, CDC37). HSP90s interact with more than 100 proteins, including kinases (e.g., Raf-1), nuclear hormone receptors (e.g., oestrogen receptor), transcription factors (e.g., P53), GPCRs (e.g., CB2 receptors) and ion channels (e.g. CFTR). In humans, the HSP90-beta isoform is constitutively expressed (i.e., at baseline), whereas HSP90-alpha isoforms are induced by stress. HSP90 plays an important role in some tumour cell types by stabilising mutated oncogenic proteins.
References in periodicals archive ?
This finding disfavors that a dependency of WT1 stability on HSP90 (Bansal et al., 2010) is linked to HDAC6.
Chemical structures of (a) PARP1 labeled with BODIPY (abs = 507 nm and em = 525 nm) and (b) Hsp90 inhibitor HS-196 labeled with FITC.
Fragment screening by weak affinity chromatography: comparison with established techniques for screening against HSP90. Anal Chem 2013; 85:6756-66.
Not surprisingly, in many animals nitric oxide synthase (NOS) requires an interaction with heat-shock protein 90 (HSP90) to keep the essential heme cofactor bound (Bishop and Brandhorst, 2003).
The downstream components; mitogen-activated protein kinases, Hsp90 and calmodulins are involved in the activation of Heat-shock transcription factors (Hsf).
& Risueno, M.C., Hsp70 and Hsp90 change their expression and subcellular localization after microspore embryogenesis induction in Brassica napus L.
Report is also available in abating HSP expression (HSP70 and HSP90) due to transportation stress lowering muscle pH and higher drip loss [5].
In the "plant-pathogen interaction pathway," three unigenes encoding the molecular chaperone heat shock protein (HSP90) functioning in the hypersensitive response (HR), K09487 (c100585.graph_c0; c155839.graph_c0), and K04079 (c124009.graph_c0) were identified (Figure 8).