Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: an update |
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Authors: | Soldani C Scovassi A Ivana |
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Affiliation: | (1) Dipartimento di Biologia Animale, University of Pavia, Piazza Botta 10, Italy;(2) Istituto di Genetica Molecolare CNR, Via Abbiategrasso 207, 27100 Pavia, Italy |
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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 NAD+ 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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Keywords: | apoptosis autoimmunity caspases PARP-1 |
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