...Xiaoyan Zhang; Andreas Brachner; Eva Kukolj; Dea Slade; Yanzhuang Wang ABSTRACT Sirtuin 2 (SIRT2) is an NAD-dependent sirtuin deacetylase that regulates microtubule and chromatin dynamics, gene expression and cell cycle progression, as well as nuclear envelope reassembly. Recent proteomic analyses...

...Tanja Kaufmann; Eva Kukolj; Andreas Brachner; Etienne Beltzung; Melania Bruno; Sebastian Kostrhon; Susanne Opravil; Otto Hudecz; Karl Mechtler; Graham Warren; Dea Slade ABSTRACT Sirtuin 2 (SIRT2) is an NAD-dependent deacetylase known to regulate microtubule dynamics and cell cycle progression...

...Renate Hvidsten Skoge; Mathias Ziegler ABSTRACT Deacetylation of α-tubulin at lysine 40 is catalyzed by two enzymes, the NAD-dependent deacetylase SIRT2 and the NAD-independent deacetylase HDAC6, in apparently redundant reactions. In the present study, we tested whether these two enzymes might have...

... indicate that Fry promotes MT acetylation in the mitotic spindle. We also found that Fry binds to the tubulin deacetylase SIRT2, preferentially in mitotic cells. Cell-free experiments revealed that the N-terminal region of Fry is the domain responsible for binding to and inhibiting the tubulin-deacetylase...

... SIRT2 as a deacetylase of the transcription factor p65. SIRT2 is a member of the family of sirtuins, which are NAD + -dependent deacetylases involved in several cellular processes. SIRT2 interacts with p65 in the cytoplasm and deacetylates p65 in vitro and in vivo at Lys310. Moreover, p65...