ArticleThe Biochemical journal2005
Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Exploring the interplay between PARP1 and circRNA biogenesis and function.Wiley interdisciplinary reviews. RNA · 2023Review
- The multifaceted role of PARP1 in RNA biogenesis.Wiley interdisciplinary reviews. RNA · 2021Review
- Poly(ADP-ribosyl)ation-dependent Transient Chromatin Decondensation and Histone Displacement following Laser Microirradiation.The Journal of biological chemistry · 2016Article
- Post-transcriptional regulation by poly(ADP-ribosyl)ation of the RNA-binding proteins.International journal of molecular sciences · 2013Review
- The fragile x mental retardation syndrome 20 years after the FMR1 gene discovery: an expanding universe of knowledge.The Clinical biochemist. Reviews · 2011Article
- Conserved genes act as modifiers of invertebrate SMN loss of function defects.PLoS genetics · 2010Article
- Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry.Proteome science · 2010Article
- Mutational analysis of the poly(ADP-ribosyl)ation sites of the transcription factor CTCF provides an insight into the mechanism of its regulation by poly(ADP-ribosyl)ation.Molecular and cellular biology · 2010Article
- Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes.Nucleic acids research · 2008Article
- Poly(ADP-ribose) glycohydrolase silencing protects against H2O2-induced cell death.The Biochemical journal · 2006Article
- Regulation of RNA splicing by the methylation-dependent transcriptional repressor methyl-CpG binding protein 2.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PARG [poly(ADP-ribose) glycohydrolase] is the only known enzyme that catalyses the hydrolysis of poly(ADP-ribose), a branched polymer that is synthesized by the poly(ADP-ribose) polymerase family of enzymes. Poly(ADP-ribosyl)ation is a transient post-translational modification that alters the functions of the acceptor proteins. It has mostly been studied in the context of DNA-damage signalling or DNA transaction events, such as replication and transcription reactions. Growing evidence now suggests that poly(ADP-ribosyl)ation could have a much broader impact on cellular functions. To elucidate the roles that could be played by PARG, we performed a proteomic identification of PARG-interacting proteins by mass spectrometric analysis of PARG pulled-down proteins. In the present paper, we report that PARG is resident in FMRP (Fragile-X mental retardation protein)-associated messenger ribonucleoparticles complexes. The localization of PARG in these complexes, which are components of the translation machinery, was confirmed by sedimentation and microscopy analysis. A functional link between poly(ADP-ribosyl)ation modulation and FMRP-associated ribonucleoparticle complexes are discussed in a context of translational regulation.
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