REVIEW: Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases

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Elizaveta E. Alemasova¹, Konstantin N. Naumenko¹, Maria V. Sukhanova¹, and Olga I. Lavrik^1,2,a*

¹Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia

²Novosibirsk State University, 630090 Novosibirsk, Russia

^* To whom correspondence should be addressed.

Received August 13, 2021; Revised September 14, 2021; Accepted September 17, 2021

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Poly(ADP-ribosyl)ation is a post-translational modification of proteins that performs an essential regulatory function in the cellular response to DNA damage. The key enzyme synthesizing poly(ADP-ribose) (PAR) in the cells is poly(ADP-ribose) polymerase 1 (PARP1). Understanding the mechanisms of the PARP1 activity regulation within the cells is necessary for development of the PARP1-targeted antitumor therapy. This review is devoted to the studies of the role of the RNA-binding protein YB-1 in the PARP1-catalyzed PARylation. The mechanisms of PARP1 activity stimulation by YB-1 protein can possibly be extended to other RNA-binding proteins involved in the maintenance of the genome stability.

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KEY WORDS: Y-box-binding protein 1 (YB-1), poly(ADP-ribosyl)ation (PARylation), poly(ADP-ribose) (PAR), poly(ADP-ribose) polymerase 1 (PARP1), RNA-binding protein (RBP)

DOI: 10.1134/S0006297922140048

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