Multiple Roles for Mono- and Poly(ADP-Ribose) in Regulating Stress Responses
| Autor: | Hongyun Qi, Brendan D. Price, Tovah A. Day |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Poly Adenosine Diphosphate Ribose
DNA damage Poly ADP ribose polymerase Article 03 medical and health sciences chemistry.chemical_compound ADP-Ribosylation 0302 clinical medicine Protein Domains Stress Physiological Cellular stress response Ribose Genetics Polymerase 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology Proteins Metabolism Cell biology Enzyme chemistry biology.protein Protein Processing Post-Translational 030217 neurology & neurosurgery Function (biology) DNA Damage Signal Transduction |
| Zdroj: | Trends in Genetics. 35:159-172 |
| ISSN: | 0168-9525 |
| DOI: | 10.1016/j.tig.2018.12.002 |
| Popis: | Although stress-induced synthesis of mono(ADP-ribose) (mADPr) and poly(ADP-ribose) (pADPr) conjugates by pADPr polymerase (PARP) enzymes has been studied extensively, the removal and degradation of pADPr, as well as the fate of ADPr metabolites, have received less attention. The observations that stress-induced pADPr undergoes rapid turnover, and that deficiencies in ADPr degradation phenocopy loss of pADPr synthesis, suggest that ADPr degradation is fundamentally important to the cellular stress response. Recent work has identified several distinct families of pADPr hydrolases that can degrade pADPr to release pADPr or mADPr into the cytoplasm. Further, many stress-response proteins contain ADPr-binding domains that can interact with these metabolites. We discuss how pADPr metabolites generated during pADPr degradation can function as signaling intermediates in processes such as inflammation, apoptosis, and DNA damage responses. These studies highlight that the full cycle of ADPr metabolism, including both synthesis and degradation, is necessary for responses to genotoxic stress. |
| Databáze: | OpenAIRE |
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