title: Towards a structural understanding of PARP1 activation and related signalling ADP-ribosyl-transferases.
abstract: ADP-ribosylation is a post-translational modification of proteins that occurs mostly in response to cellular stress and is catalysed by members of the diverse poly-ADP-ribose (PAR) polymerase (PARP/ARTD) family. The founding member of the family, PARP1, is best recognized for its function as a sensor of DNA strand lesions, but ADP-ribosylation has been implicated in transcriptional regulation, chromatin dynamics, telomere maintenance, apoptosis and neuronal signalling. Here we summarize a number of exciting recent breakthroughs in our understanding of the structural and mechanistic aspects of how PARP1 recognizes DNA, how PARPs are regulated, how ADP-ribose modifications are set onto specific targets and how the cellular machinery recognizes this elusive post-translational modification.
authors.affiliation: Department of Physiological Chemistry, LMU BioMedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5B, 81377 Munich, Germany.
authors.forename: Markus
authors.initials: M
authors.lastname: Hassler
authors.forename: Andreas G
authors.initials: AG
authors.lastname: Ladurner
mesh_terms: D036002:ADP Ribose Transferases / Q000378:metabolism*; D000818:Animals; D055162:Biocatalysis; D004789:Enzyme Activation; D006801:Humans; D011065:Poly(ADP-ribose) Polymerases / Q000737:chemistry* / Q000378:metabolism*; D015398:Signal Transduction; D013379:Substrate Specificity
chemical_list: D036002:ADP Ribose Transferases; D011065:Poly(ADP-ribose) Polymerases