Reactome | SIRT6 deacetylates RBBP8

SIRT6 deacetylates RBBP8

Stable Identifier

R-HSA-5685953

Type

Reaction [uncertain]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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