A fast signal-induced activation of poly(ADP-ribose) polymerase: A novel downstream target of phospholipase C

S. Homburg, L. Visochek, N. Moran, F. Dantzer, E. Priel, E. Asculai, D. Schwartz, V. Rotter, N. Dekel, M. Cohen-Armon

Research output: Contribution to journalArticlepeer-review

136 Scopus citations

Abstract

We present the first evidence for a fast activation of the nuclear protein poly(ADP-ribose) polymerase (PARP) by signals evoked in the cell membrane, constituting a novel mode of signaling to the cell nucleus. PARR an abundant, highly conserved, chromatin-bound protein found only in eukaryotes, exclusively catalyzes polyADP-ribosylation of DNA-binding proteins, thereby modulating their activity. Activation of PARR reportedly induced by formation of DNA breaks, is involved in DNA transcription, replication, and repair. Our findings demonstrate an alternative mechanism: a fast activation of PARR evoked by inositol 1,4,5,-trisphosphate-Ca2+ mobilization, that does not involve DNA breaks. These findings identify PARP as a novel downstream target of phospholipase C, and unveil a novel fast signal-induced modification of DNA-binding proteins by polyADP-ribosylation.

Original languageEnglish
Pages (from-to)293-307
Number of pages15
JournalJournal of Cell Biology
Volume150
Issue number2
DOIs
StatePublished - 24 Jul 2000

Keywords

  • Brain neurons
  • Calcium signaling
  • Electrical stimulation
  • Inositol 1,4,5- trisphosphate
  • Poly(ADP-ribose) polymerase

ASJC Scopus subject areas

  • Cell Biology

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