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• W2051569143 abstract "Huntington´s disease, one of the so-called poly-glutamine diseases, is a dominantly inherited movement disorder characterized by formation of cytosolic and nuclear inclusion bodies and progressive neurodegeneration. Recently, we have shown that Bcl-2-associated athanogene-1 (BAG1), a multifunctional co-chaperone, modulates toxicity, aggregation, degradation and subcellular distribution in vitro and in vivo of the disease-specific mutant huntingtin protein. Aiming at future small molecule-based therapeutical approaches, we further analysed structural demands for these effects employing the C-terminal deletion mutant BAGDC. We show that disruption of the BAG domain known to eliminate intracellular heat shock protein 70 (Hsp70) binding and activation also precludes binding of Siah-1 thereby leaving nuclear huntingtin translocation unaffected. At the same time BAGDC fails to induce increased proteasomal huntingtin turnover and does not inhibit intracellular huntingtin aggregation, a pre-requisite necessary for prevention of huntingtin toxicity." @default.
• W2051569143 created "2016-06-24" @default.
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• W2051569143 date "2010-09-28" @default.
• W2051569143 modified "2023-09-25" @default.
• W2051569143 title "Modulation of Huntingtin Toxicity by BAG1 is Dependent on an Intact BAG Domain" @default.
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• W2051569143 doi "https://doi.org/10.3390/molecules15106678" @default.
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