May 29, 2020 · In contrast, activation of SIRT1 increased autophagy in chondrocytes by the deacetylation of lysine residues on crucial autophagy proteins (Beclin1, ATG5, ATG7, LC3). This activation was shown...

Mar 29, 2024 · Sirt1 deacetylates the lysine residues on ATG7 and other crucial autophagy proteins to increase autophagy in chondrocytes. Chondrocyte-specific Sirt1 silencing decreases chondrogenic markers.

Mar 4, 2008 · We further demonstrate that Sirt1 can form a molecular complex with several essential components of the autophagy machinery, including autophagy genes (Atg)5, Atg7, and Atg8. In vitro, Sirt1 can, in an NAD-dependent fashion, directly deacetylate these components.

Sep 28, 2020 · Here we report that macroautophagy (hereafter referred to as autophagy), a catabolic membrane trafficking pathway that degrades cellular components through autophagosomes and lysosomes, mediates...

Jan 1, 2024 · SIRT1-mediated deacetylation of ATGs (e.g., ATG5, ATG7, ATG8, and ATG12) is critical for the activation of autophagy, and SIRT1 regulates the elongation and maturation of autophagosomes through this deacetylation function.

These results suggest that Sirt1 in human chondrocytes regulates autophagy by interacting with autophagy related Atg7, and Sirt1 may become a more important target in OA treatment.

Sirt1 extends lifespan in lower organisms, whereas it suppresses aging-induced cardiomyopathy and protects against oxidative stress in the mouse heart. 8 Sirt1 regulates autophagy by interacting with autophagy related genes Atg5, Atg7, and Atg8 and deacetylating them.

Considering that the acetylation of ATG7 is determined by acetyltransferase EP300-CREBBP and deacetylase SIRT1 [21,22], it would need further investigation to clarify the role of EP300-CREBBP and SIRT1 in controlling the acetylation of ATG7 in …

Mar 4, 2008 · We further demonstrate that Sirt1 can form a molecular complex with several essential components of the autophagy machinery, including autophagy genes (Atg)5, Atg7, and Atg8. In vitro, Sirt1 can, in an NAD-dependent fashion, directly deacetylate these components.

Dec 20, 2020 · First, inhibition of autophagy by ATG7 knockdown prevents SIRT1 downregulation in senescent cells. Second, using imaging experiments, we found that while SIRT1 in proliferating primary human fibroblasts is localized in the nucleus, SIRT1 undergoes nucleus-to-cytoplasm shuttling and is targeted by phagophores (autophagosome precursors) and ...