Mutations in the acetylation hotspots of Rbl2 are associated with increased risk of breast cancer.

ABSTRACT: Retinoblastoma like protein-2 (Rbl2) is functionally regulated by phosphorylation and acetylation. Previously, we demonstrated that lysine K1083 (K1079 in human Rbl2) is a potential target for acetylation but its functional role remains elusive. We investigated alterations in human Rbl2 gene specifically targeting exons 19-22 harbouring acetylatable residues i.e. K1072, K1083 and K1115 through single stranded conformation polymorphism (SSCP) in breast cancer patients. The K1083 was found altered into arginine (R) in 51% of the cases but K1072 and K1115 remained conserved. The 'K1083R' mutation impairs the acetylation potential of this motif that may result in functional inactivation of Rbl2. These patients also showed poor survival outcome that highlights prognostic relevance of this resid

SUBMITTER: Ullah F 

PROVIDER: S-EPMC8985964 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature