期刊
JOURNAL OF CELL BIOLOGY
卷 150, 期 2, 页码 293-307出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.150.2.293
关键词
poly(ADP-ribose) polymerase; calcium signaling; inositol 1,4,5-trisphosphate; electrical stimulation; brain neurons
类别
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. PARP, 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 PARP, 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 PARP, 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 poly ADP-ribosylation.
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