TY - JOUR
T1 - Poly(ADP-ribose) polymerase-1 cleavage during apoptosis
T2 - An update
AU - Soldani, C.
AU - Scovassi, A. I.
PY - 2002
Y1 - 2002
N2 - 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 arefurther 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.
AB - 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 arefurther 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.
KW - Apoptosis
KW - Autoimmunity
KW - Caspases
KW - PARP-1
UR - http://www.scopus.com/inward/record.url?scp=0036022402&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036022402&partnerID=8YFLogxK
U2 - 10.1023/A:1016119328968
DO - 10.1023/A:1016119328968
M3 - Article
C2 - 12101391
AN - SCOPUS:0036022402
VL - 7
SP - 321
EP - 328
JO - Apoptosis : an international journal on programmed cell death
JF - Apoptosis : an international journal on programmed cell death
SN - 1360-8185
IS - 4
ER -