Ontology highlight
ABSTRACT:
SUBMITTER: Krzysiak TC
PROVIDER: S-EPMC6309500 | biostudies-literature | 2018 Dec
REPOSITORIES: biostudies-literature
Krzysiak Troy C TC Thomas Laurel L Choi You-Jin YJ Auclair Sylvain S Qian Yiqi Y Luan Shan S Krasnow Stephanie M SM Thomas Laura L LL Koharudin Leonardus M I LMI Benos Panayiotis V PV Marks Daniel L DL Gronenborn Angela M AM Thomas Gary G
Molecular cell 20181108 6
Current models of SIRT1 enzymatic regulation primarily consider the effects of fluctuating levels of its co-substrate NAD<sup>+</sup>, which binds to the stably folded catalytic domain. By contrast, the roles of the sizeable disordered N- and C-terminal regions of SIRT1 are largely unexplored. Here we identify an insulin-responsive sensor in the SIRT1 N-terminal region (NTR), comprising an acidic cluster (AC) and a 3-helix bundle (3HB), controlling deacetylase activity. The allosteric assistor D ...[more]