Poly(ADP-ribose) polymerase-1 cleavage during apoptosis

An update

C. Soldani, A. I. Scovassi

Research output: Contribution to journalArticle

485 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)321-328
Number of pages8
JournalApoptosis
Volume7
Issue number4
DOIs
Publication statusPublished - 2002

Fingerprint

Poly Adenosine Diphosphate Ribose
Poly(ADP-ribose) Polymerases
Adenosine Diphosphate
Adenosine Diphosphate Ribose
Apoptosis
Single-Stranded DNA Breaks
DNA
Post Translational Protein Processing
Caspases
Nuclear Proteins
DNA Repair
NAD
Proteolysis
Polymers
Cell Death
Cell death
Peptides
Catalyst activity
Repair
Enzymes

Keywords

  • Apoptosis
  • Autoimmunity
  • Caspases
  • PARP-1

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Cell Biology

Cite this

Poly(ADP-ribose) polymerase-1 cleavage during apoptosis : An update. / Soldani, C.; Scovassi, A. I.

In: Apoptosis, Vol. 7, No. 4, 2002, p. 321-328.

Research output: Contribution to journalArticle

Soldani, C. ; Scovassi, A. I. / Poly(ADP-ribose) polymerase-1 cleavage during apoptosis : An update. In: Apoptosis. 2002 ; Vol. 7, No. 4. pp. 321-328.
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