IndraLab

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ATXN3 activates autophagy. 16 / 16
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"Paradoxically, in a fly model of SCA3 (another polyQ disease), flies expressing pathogenic SCA3 (SCA3trQ78) display increased autophagy and neurodegenerative phenotypes, indicating that increased autophagy may promote the disease."
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"Ataxin-3, another deubiquitinating enzyme is involved in deubiquitinating K48-linked poly-ubiquitin chains from BECN1-K402, thus stabilizing BECN1 and promoting starvation-induced autophagy (Ashkenazi et al., 2017)."
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"First, we determined whether normal or pathogenic Ataxin-3 itself induced lysosomal accumulation reflective of autophagy, by examining the fat body tissue from larvae, a standard assay for autophagy [XREF_BIBR]."
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"Together , we conclude that ATXN3 stimulates autophagy and thereby optimizes the cellular response to nutrient starvation and proteotoxic stress , two conditions that rely heavily on autophagy ."
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"While Ataxin-3 deficient cells are still able to induce autophagy, the induction process appeared to be exaggerated with an increased number of autophagosomes, which is accompanied by less efficient turnover of proteins by autophagy."
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"No change in the number of LC3-II vesicles was observed when the Q35 tract was expressed in beclin 1 depleted cells (XREF_FIG) and the inhibitory effect of Q35 on beclin 1 levels and autophagy in beclin 1 expressing cells was rescued by ataxin-3 overexpression (XREF_FIG), compatible with the model that the Q35 acts by impairing ataxin-3 control of beclin 1 levels."
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"Furthermore, pathogenic ATXN3 induces autophagy in a Drosophila model."
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"Treatment of the larval SCA3 zebrafish with various compounds with autophagy induction capacity was able to produce the improved swimming of the zebrafish, suggesting the potential benefit of autophagy-inducing compounds for the treatment of SCA3."
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"The normal function of Ataxin-3 is in ubiquitin modulated pathways [XREF_BIBR - XREF_BIBR]; our data suggest the possibility that Ataxin-3 may also modulate autophagy."
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"According with the literature, the polyQ stretch in wild-type ataxin-3 induces autophagy by protecting Beclin-1 from proteasome-mediated degradation (Ashkenazi et al., 2017)."
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"This may arise from beclin-1 degradation caused by expanded mutant ataxin-3 polyQ , whereas normal ataxin-3 promotes autophagy by preventing proteosome degradation of beclin-1 [ 77,78 ] ."
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"Interestingly, early studies indicated that proteins containing PolyQ, for example, Ataxin-3, might interact with Beclin 1 to promote the autophagy [XREF_BIBR], and AR proteins with different PolyQ lengths have been reported to have different transactivation capacity to modulate AR target genes [XREF_BIBR, XREF_BIBR, XREF_BIBR]."
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"Since autophagy can mediate the clearance of polyQ expanded ataxin-3, we presumed that the over-expression of ataxin-3 alone is sufficient to induce autophagy."
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"An independent study described a similar induction of autophagy by Ataxin-3 in Drosophila, suggesting that induction of autophagy by pathogenic aggregates is a common phenomenon in neurodegenerative diseases [XREF_BIBR]."
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"Pathogenic Ataxin-3 Stimulates Autophagy, with Select Modifiers Promoting and Others Preventing Autophagy."
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"Valproate treatment of the MJD zebrafish resulted in increased levels of beclin-1, p62 and LC3II compared to the vehicle-treated control (Fig. 6A–D), supporting increased autophagy induction."
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