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HSPB8 binds BAG3 to promote spatial sequestration of ubiquitinated proteins.
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results strongly suggest that HSP22 represses HCC progression, especially HCC cell migration, by the down-regulation of the PI3K/AKT signaling pathway.
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We identified impaired RNA metabolism, secondary to TDP-43 loss of function, as a possible pathological mechanism of HSPB8 toxicity, leading to muscle and nerve degeneration
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Data indicated that the HSPB8 expression level was strongly positively correlated with MAPK signaling pathway and CREB pathway and worse prognosis. The methylation level of its DNA was negatively associated with its expression and positively associated with overall survival. These results suggest that HSPB8 could promote the proliferation and inhibit the apoptosis of GC cells by activating ERKCREB signaling.
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HSPB2 competes with HSPB8 for binding to BAG3. In contrast, HSPB3 negatively regulates HSPB2 association with BAG3.
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Silencing of HSPB8 markedly decreased the mitotic levels of BAG3 in HeLa cells, supporting its crucial role in BAG3 mitotic functions. The results support a role for the HSPB8-BAG3 chaperone complex in quality control of actin-based structure dynamics that are put under high tension, notably during cell cytokinesis.
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HSPB8 is involved in regulating the cell cycle and cell migration in MCF-7 cells.
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suggest that HSPB8 may act as an intracellular factor against hepatitis C virus replication and that DNAJC5B has the same function, with more relevant results for genotype 3
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It has been demonstrated that HSPB8-BAG3-HSP70 ensures the functionality of stress granules and restores proteostasis by targeting defective ribosomal products for degradation.
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We report that overexpression of HSPB8 in immortalized motor neurones decreased the accumulation of TDP-25 and TDP-35 and that protection against mislocalized/truncated TDP-43 was observed for HSPB8 in Drosophila melanogaster Overexpression of HSP67Bc, the functional ortholog of human HSPB8, suppressed the eye degeneration caused by the cytoplasmic accumulation of a TDP-43 variant
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HSPB8 counteracts accumulation of aberrantly localized misfolded forms of TDP-43 and its 25 KDa fragment involved in most sporadic cases of Amyotrophic Lateral Sclerosis and of Fronto Lateral Temporal Dementia.
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expands the understanding of disease mechanisms, tissue involvement, and phenotypic outcome of HSPB8 mutations
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our findings suggest the existence of a so-far unrecognized quality control mechanism involving BAG3, HSPB8 and p62/SQSTM1 for accurate remodelling of actin-based mitotic structures that guide spindle orientation.
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This study demonstreated that expression of HSPB8 was restricted to GFAP+ astrocytes in patient with multiple sclerosis.
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Pangenomic profiling of velcade-sensitive and resistant cells showed that the small heat shock protein HSPB8 was overexpressed in multiple myeloma resistant cells.
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HSP22 acts as a positive regulator in TGF-alpha-induced migration of ovarian cancer cells, subsequently directing ovarian cancer toward progression.
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HSP22 plays an important role on gastric tumor aggressiveness and prognosis and may act as a promising target for prognostic prediction.
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Mutant HSPB8 causes protein aggregates and a reduced mitochondrial membrane potential in dermal fibroblasts from distal hereditary motor neuropathy patients.
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The expression of HspB8 inhibits the growth of genetically diverse melanoma cells that include caspase-1 activation outside of the realm of the inflammasome, mTORC1-dependent Beclin-1 upregulation and its cleavage by the activated caspase-1.
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findings show that during heat shock recovery NF-kappaB activates selective removal of misfolded or aggregated proteins by controlling expression of BAG3 and HSPB8 and by modulating the level of the BAG3-HspB8 complex
