Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm

Since its discovery in 1963, poly(ADP-ribose) (pADPr) has been shown to play important functions in the nucleus of multicellular eukaryotes. Each of these functions centers upon DNA metabolism, including DNA-damage repair, chromatin remodeling, transcription and telomere functions. We recently descr...

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Bibliographic Details
Published in:RNA biology 2012-05, Vol.9 (5), p.542-548
Main Authors: Leung, Anthony K.L., Todorova, Tanya, Ando, Yoshinari, Chang, Paul
Format: Article
Language:English
Subjects:
Binding
Biology
Bioscience
Calcium
Cancer
Cell
Cycle
Cytoplasm
Cytoplasmic Granules - metabolism
Humans
Landes
microRNA
Organogenesis
PARG
PARP
PARP-13
Point of View
Poly Adenosine Diphosphate Ribose - physiology
Poly(ADP-ribose) Polymerases - metabolism
Poly(ADP-ribose) Polymerases - physiology
Protein Multimerization
Protein Processing, Post-Translational
Proteins
RNA Interference
stress
stress granule
ZAP
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Summary:Since its discovery in 1963, poly(ADP-ribose) (pADPr) has been shown to play important functions in the nucleus of multicellular eukaryotes. Each of these functions centers upon DNA metabolism, including DNA-damage repair, chromatin remodeling, transcription and telomere functions. We recently described two novel functions for pADPr in the cytoplasm, both of which involve RNA metabolism - 1) the assembly of cytoplasmic stress granules, cellular macrostructures that aggregate translationally stalled mRNA/protein complexes, and 2) modulation of microRNA activities. Multiple stress granule-localized, post-transcriptional gene regulators, including microRNA-binding argonaute family members, are substrates for pADPr modification and are increasingly modified by pADPr upon stress. Interestingly, the cytoplasmic RNA regulatory functions for PARPs are likely mediated through activities of catalytically inactive PARP-13/ARTD13/ZC3HAV1/ZAP and mono/poly(ADP-ribose)-synthesizing enzymes, including PARP-5a/ARTD5/TNKS1, PARP-12/ARTD12/ZC3HDC1 and PARP-15/ARTD7/BAL3. These data are consistent with other recent work, which suggests that mono(ADP-ribosyl)ated residues can be poly(ADP-ribosyl)ated by different enzymes.
ISSN:1547-6286
1555-8584
DOI:10.4161/rna.19899