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Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: An update

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Abstract

Poly(ADP-ribosylation) is a post-translational modification of proteins playing a crucial role in many processes, including DNA repair and cell death. The best known poly(ADP-ribosylating) enzime, PARP-1, is a DNA nick sensor and uses βNAD+ to form polymers of ADP-ribose which are further bound to nuclear protein acceptors. To strictly regulate poly(ADP-ribose) turnover, its degradation is assured by the enzyme poly(ADP-ribose) glycohydrolase (PARG). During apoptosis, PARP-1 plays two opposite roles: its stimulation leads to poly(ADP-ribose) synthesis, whereas caspases cause PARP-1 cleavage and inactivation. PARP-1 proteolysis produces an 89 kDa C-terminal fragment, with a reduced catalytic activity, and a 24 kDa N-terminal peptide, which retains the DNA binding domains. The fate and the possible role of these fragments during apoptosis will be discussed.

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  1. Dipartimento di Biologia Animale, University of Pavia, Piazza Botta 10, Italy

    C. Soldani

  2. Istituto di Genetica Molecolare CNR, Via Abbiategrasso 207, 27100, Pavia, Italy

    A. I. Scovassi

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Soldani, C., Scovassi, A.I. Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: An update. Apoptosis 7, 321–328 (2002). https://doi.org/10.1023/A:1016119328968

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