Polyglutamine tracts regulate beclin 1-dependent autophagy

Avraham Ashkenazi, Carla F. Bento, Thomas Ricketts, Mariella Vicinanza, Farah Siddiqi, Mariana Pavel, Ferdinando Squitieri, Maarten C. Hardenberg, Sara Imarisio, Fiona M. Menzies and David C. Rubinsztein ()
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Avraham Ashkenazi: Cambridge Institute for Medical Research (CIMR), University of Cambridge
Carla F. Bento: Cambridge Institute for Medical Research (CIMR), University of Cambridge
Thomas Ricketts: Cambridge Institute for Medical Research (CIMR), University of Cambridge
Mariella Vicinanza: Cambridge Institute for Medical Research (CIMR), University of Cambridge
Farah Siddiqi: Cambridge Institute for Medical Research (CIMR), University of Cambridge
Mariana Pavel: Cambridge Institute for Medical Research (CIMR), University of Cambridge
Ferdinando Squitieri: IRCCS Casa Sollievo della Sofferenza, Huntington and Rare Diseases Unit
Maarten C. Hardenberg: Cambridge Institute for Medical Research (CIMR), University of Cambridge
Sara Imarisio: Cambridge Institute for Medical Research (CIMR), University of Cambridge
Fiona M. Menzies: Cambridge Institute for Medical Research (CIMR), University of Cambridge
David C. Rubinsztein: Cambridge Institute for Medical Research (CIMR), University of Cambridge

Nature, 2017, vol. 545, issue 7652, 108-111

Abstract: The polyglutamine domain in ataxin 3, which is expanded in spinocerebellar ataxia type 3, allows normal ataxin 3 to interact with and deubiquitinate beclin 1 and thereby to promote autophagy.

Date: 2017
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DOI: 10.1038/nature22078

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