Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation

Current Opinion in Cell Biology

Volumn 20, Issue 3, 2008, Pages 294-302

  Kraus, W Lee ^a  

^a Department of Molecular Biology and Genetics   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; BRCA1 PROTEIN; CYTOKINE; DNA BINDING PROTEIN; DNA METHYLTRANSFERASE; HEAT SHOCK PROTEIN; HISTONE; HISTONE DEACETYLASE 3; HORMONE; MITOGEN ACTIVATED PROTEIN KINASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NUCLEAR PROTEIN;

ACETYLATION; BINDING AFFINITY; CELL NUCLEUS MATRIX; CHROMATIN STRUCTURE; DNA BINDING; DNA METHYLATION; ENZYME ACTIVITY; GENE EXPRESSION REGULATION; HUMAN; NONHUMAN; NUCLEOSOME; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN FUNCTION; REVIEW; TRANSCRIPTION REGULATION;

ADENOSINE DIPHOSPHATE RIBOSE; ANIMALS; DNA-BINDING PROTEINS; ENHANCER ELEMENTS (GENETICS); GENE EXPRESSION REGULATION; GENOME; HUMANS; POLY ADENOSINE DIPHOSPHATE RIBOSE; POLY(ADP-RIBOSE) POLYMERASES; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; TRANSCRIPTION, GENETIC;

EID: 44649130038     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2008.03.006     Document Type: Review

References (62)

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57. ••]. This paper first, demonstrates that direct phosphorylation of PARP-1 by ERK1/2 can enhance PARP-1 activity and second, identifies ERK1/2 phosphorylation sites on PARP-1 by mass spectrometry and site-directed mutagenesis. Although ERK1/2 pathway inhibitors blocked PARP-1 activation and PARP-1-mediated neuronal death, the effects on PARP-1-dependent gene expression were not determined.
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60. + synthase NMNAT-1 in the regulation of PARP-1 enzymatic activity. Specifically, the results show that NMNAT-1 stimulates PARP-1 automodification, as well as binds to PAR. Phosphorylation of NMNAT-1 by protein kinase C reduces its binding to PAR, suggesting that NMNAT-1 may be an endpoint of cell signaling pathways. Together, these results demonstrate that NMNAT-1 can enhance the activity of PARP-1 and, thus, amplify PARylation.
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