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10.1080/15548627.2017.1336278 http://scihub22266oqcxt.onion/10.1080/15548627.2017.1336278 C5612341!5612341!28722507     free     free     free       Autophagy 2017 ; 13 (9): 1613-4 Nephropedia Template TP {{tp|p=28722507|t=2017. Polyglutamine tracts regulate autophagy |pdf=|usr=}}{{28722507}} gab.com Text Polyglutamine tracts regulate autophagy JO: Autophagy http://www.kidney.de/pget.php?&tw=1&pmid=28722507 #FOAvip Expansions of polyglutamine (polyQ) tracts in different proteins cause 9 neurodegenerative conditions, such as Huntington disease and various ataxias. However, many normal mammalian proteins contain shorter polyQ tracts. As these are frequently conserved in multiple species, it is likely that some of these polyQ tracts have important but unknown biological functions. Here we review our recent study showing that the polyQ domain of the deubiquitinase ATXN3/ataxin-3 enables its interaction with BECN1/beclin 1, a key macroautophagy/autophagy initiator. ATXN3 regulates autophagy by deubiquitinating BECN1 and protecting it from proteasomal degradation. Interestingly, expanded polyQ tracts in other polyglutamine disease proteins compete with the shorter ATXN3 polyQ stretch and interfere with the ATXN3-BECN1 interaction. This competition results in decreased BECN1 levels and impaired starvation-induced autophagy, which phenocopies the loss of autophagic function mediated by ATXN3. Our findings describe a new autophagy-protective mechanism that may be altered in multiple neurodegenerative diseases. Twit Text FOAVip Polyglutamine tracts regulate autophagy ????Autophagy http://www.kidney.de/pget.php?&tw=1&pmid=28722507 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28722507 #FOAvip English Wikipedia <ref>{{Cite pmid|28722507}}</ref> Polyglutamine tracts regulate autophagy #MMPMID28722507 Ashkenazi A; Bento CF; Ricketts T; Vicinanza M; Siddiqi F; Pavel M; Squitieri F; Hardenberg MC; Imarisio S; Menzies FM; Rubinsztein DC Autophagy 2017[]; 13 (9): 1613-4 PMID28722507show ga Expansions of polyglutamine (polyQ) tracts in different proteins cause 9 neurodegenerative conditions, such as Huntington disease and various ataxias. However, many normal mammalian proteins contain shorter polyQ tracts. As these are frequently conserved in multiple species, it is likely that some of these polyQ tracts have important but unknown biological functions. Here we review our recent study showing that the polyQ domain of the deubiquitinase ATXN3/ataxin-3 enables its interaction with BECN1/beclin 1, a key macroautophagy/autophagy initiator. ATXN3 regulates autophagy by deubiquitinating BECN1 and protecting it from proteasomal degradation. Interestingly, expanded polyQ tracts in other polyglutamine disease proteins compete with the shorter ATXN3 polyQ stretch and interfere with the ATXN3-BECN1 interaction. This competition results in decreased BECN1 levels and impaired starvation-induced autophagy, which phenocopies the loss of autophagic function mediated by ATXN3. Our findings describe a new autophagy-protective mechanism that may be altered in multiple neurodegenerative diseases. äPolyglutamine tracts regulate autophagy (epmc).pdf DeepDyve Pubget Overpricing