SIRT6 deacetylates RBBP8

Stable Identifier
Reaction [uncertain]
Homo sapiens
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Deacteylation of RBBP8 (CtIP) upon DNA damage is dependent on SIRT6 protein lysine deacetylase and positively regulated by Lamin A (LMNA), where LMNA is thought to facilitate localization of SIRT6 to damaged DNA (Ghosh et al. 2015). SIRT6 depletion is associated with increased acetylateion of RBBP8 and impaired DNA repair (Cagnetta et al. 2018). Increased level of SIRT6 correlates with deacetylation of RBBP8 (Wang et al. 2022).

Literature References
PubMed ID Title Journal Year
29025907 Depletion of SIRT6 enzymatic activity increases acute myeloid leukemia cells' vulnerability to DNA-damaging agents

Duchosal, M, Lemoli, RM, Talarico, G, Cea, M, Soncini, D, Retali, V, Gobbi, M, Nahimana, A, Orecchioni, S, Minetto, P, Clavio, M, Bergamaschi, M, Todoerti, K, Carminati, E, Cagnetta, A, Colombo, N, Bertolini, F, Nencioni, A, Bruzzone, S, Neri, A, Miglino, M, Guolo, F, Passalacqua, M

Haematologica 2018
36172813 The mechanism of radiotherapy for lung adenocarcinoma in promoting protein SIRT6-mediated deacetylation of RBBP8 to enhance the sensitivity of targeted therapy

Sheng, Z, Cai, Y, Wu, Q, Wang, J, Dong, Z

Int J Immunopathol Pharmacol 2022
26549451 Lamin A Is an Endogenous SIRT6 Activator and Promotes SIRT6-Mediated DNA Repair

Ghosh, S, Hao, Q, Wang, Y, Zhou, Z, Liu, B

Cell Rep 2015
Catalyst Activity

NAD-dependent protein deacetylase activity of SIRT6 [nucleoplasm]

Orthologous Events
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