Poly(ADP-ribose) Polymerase 1 Interacts with Nuclear Respiratory Factor 1 (NRF-1) and Plays a Role in NRF-1 Transcriptional Regulation

Hossain, Mohammad B.; Ji, Ping; Anish, Ramakrishnan; Jacobson, Raymond H.; Takada, Shinako

doi:10.1074/jbc.m807198200

Cited by 51 publications

(51 citation statements)

References 38 publications

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“…NRF-1, in complex with DNA-dependent protein kinase (DNA-PK), Ku80, Ku70, and topoisomerase Iib, was shown to bind to PARP-1 [57]. PARP-1 binds to and PARylates the DNA binding domain of NRF1, however PARylated NRF-1 does not lose its affinity to PARP-1 [57].…”

Section: Reviewmentioning

confidence: 99%

“…PARP-1 binds to and PARylates the DNA binding domain of NRF1, however PARylated NRF-1 does not lose its affinity to PARP-1 [57]. The NRF-1/PARP-1 complex binds to the human cytochrome c promoter and facilitates cytochrome c expression [57].…”

Section: Reviewmentioning

confidence: 99%

“…Some of these pathways are independent of PARylation (e.g., NRFs [57,58]), and are hence capable of preserving mitochondrial activity under stress conditions. These feedforward pathways might be important for cells to recover from sublethal PARP-mediated stress situations [42,49,50].…”

Section: Concluding Remarks and Future Perspectivesmentioning

confidence: 99%

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Poly(ADP-ribose) polymerases as modulators of mitochondrial activity

Bai

Nagy

Fodor

et al. 2015

Trends in Endocrinology & Metabolism

100

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Activation of poly(ADP-ribose) polymerases-1 and -2 (PARP-1 and PARP-2) deteriorates mitochondrial activity. NAD + and ATP degradation are not coupled to each other upon PARP activation. PARPs interact with transcription factors modulating mitochondrial activity. PARPs can be positive regulators of mitochondrial output under sublethal stress. PARP inhibition is an attractive target for treating mitochondrial dysfunction.

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Section: Reviewmentioning

confidence: 99%

Section: Reviewmentioning

confidence: 99%

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Poly(ADP-ribose) polymerases as modulators of mitochondrial activity

Bai

Nagy

Fodor

et al. 2015

Trends in Endocrinology & Metabolism

100

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“…Nuclear respiratory factor 1 participates in cellular oxidation-reduction signaling of inflammatory responses by increasing cytochrome c expression and mitochondrial respiratory capacity. 84 The interactions of PARP-1 with NRF-1 and NRF-1 activation were regulated by automodification of PARP-1 and PARylation of NRF-1, 84 suggesting that PARP-1 plays a regulatory role in NRF-1-dependent mitochondrial biogenesis, function, and cellular oxidationreduction status. Conversely, PARP-1 may promote inflammation via negatively regulating other transcription factors.…”

Section: Role Of Parp-1 In Inflammatory Gene Expressionmentioning

confidence: 99%

Signaling Mechanism of Poly(ADP-Ribose) Polymerase-1 (PARP-1) in Inflammatory Diseases

Garg

2011

The American Journal of Pathology

171

140

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Poly(ADP-ribosyl)ation, attaching the ADP-ribose polymer chain to the receptor protein, is a unique posttranslational modification. Poly(ADP-ribose) polymerase-1 (PARP-1) is a well-characterized member of the PARP family. In this review, we provide a general update on molecular structure and structure-based activity of this enzyme. However, we mainly focus on the roles of PARP-1 in inflammatory diseases. Specifically, we discuss the signaling pathway context that PARP-1 is involved in to regulate the pathogenesis of inflammation. PARP-1 facilitates diverse inflammatory responses by promoting inflammation-relevant gene expression, such as cytokines, oxidation-reductionrelated enzymes, and adhesion molecules. Excessive activation of PARP-1 induces mitochondria-associated cell death in injured tissues and constitutes another mechanism for exacerbating inflammation. There are many posttranslational protein modifications (eg, phosphorylation, acetylation, methylation, and ubiquitylation) that are involved in a wide scope of cellular processes, including chromatin remodeling, transcriptional regulation, and signal transmission response to extracellular stimulation. Poly(ADP-ribosyl)ation (PARylation) is one of such essential protein modifications, whereby polymers of ADP-ribose (PARs) are formed from donor NAD ϩ molecules and covalently attached via an ester linkage to glutamic acid and less commonly to aspartic acid or lysine of target proteins.1-3 The target proteins generally contain a PAR-binding consensus motif that frequently overlaps with a functional domain, such as a protein-or DNA-binding domain (DBD), and thus accounts for PAR modification, altering the functional properties of the targets. 4 The process of PARylation is catalyzed by the poly-(ADP-ribose) polymerase (PARP) family of enzymes that consists of 18 members. 5 The PARPs, historically known as poly(ADP-ribose) synthases and poly(ADP-ribose) transferases, 6,7 show different structure, cellular location, and functions. 8,9 Only two members of this family (ie, PARP-1 and PARP-2) are DNA damage related; and PARP-1, the best-understood member, is an abundant nuclear enzyme and accounts for at least 85% of the cellular PARP activity. 10Since the discovery of PAR synthesis and PARP-1 decades ago, 11,12 new discoveries have been consistently published related to their structure, property, and functions. PARP-1 is a multifunctional enzyme and has a key role in the spatial and temporal organization of DNA repair, thus maintaining genome integrity and facilitating cell survival. PARP-1 catalyzes the synthesis and attachment of highly negatively charged PARs to target proteins, including histones, topoisomerases, DNA helicases, and single-strand break repair and base excision repair factors; and facilitates relaxation of the chromatin superstructure, protein-protein interaction, and DNAbinding ability of the members of the DNA repair machinery. A recently published article 13 reviews the role of PARP-1 in DNA repair. In addition, the importance of poly-(ADP-...

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“…Many studies have linked PARP-1 and Ku either directly or as components of multiprotein complexes (Ruscetti et al, 1998;Ariumi et al, 1999;Galande and Kohwi-Shigematsu, 1999;Grote et al, 2006;Yin and Glass, 2006;Hossain et al, 2009). Although cell lines' extraction procedures and coimmunoprecipitation protocols vary between studies, there have been consistent observations of Ku/PARP-1 interactions and a frequent observation that PARP activity or DNA-PK mediated phosphorylation modulates the complexes.…”

Section: Discussionmentioning

confidence: 99%

Activation of PARP-1 in response to bleomycin depends on the Ku antigen and protein phosphatase 5

Fang¹,

Soubeyrand²,

Haché

2010

Oncogene

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Poly (ADP-ribose) polymerase-1 (PARP-1) has an important role in the cellular response to a broad spectrum of DNA lesions. PARP-1 is strongly activated in response to double-stranded DNA breaks (DSBs), yet its contribution to the DSB response is poorly understood. Here we used bleomycin, a radiomimetic that generates DSBs with high specificity to focus on the response of PARP-1 to DSBs. We report that the induction of PARP-1 activity by bleomycin depends on the Ku antigen, a nonhomologous-DNA-End-Joining factor and protein phosphatase 5 (PP5). PARP-1 activation in response to bleomycin was reduced over 10-fold in Ku-deficient cells, whereas its activation in response to U.V. was unaffected. PARP-1 activation was rescued by reexpression of Ku, but was refractory to manipulation of DNA-dependent protein kinase or ATM. Similarly, PARP-1 activation subsequent to bleomycin was reduced 2-fold on ablation of PP5 and was increased 5-fold when PP5 was overexpressed. PP5 seemed to act directly on PARP-1, as its basal phosphorylation was reduced on overexpression of PP5, and PP5 dephosphorylated PARP-1 in vitro. These results highlight the functional importance of Ku antigen and PP5 for PARP-1 activity subsequent to DSBs.

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Poly(ADP-ribose) Polymerase 1 Interacts with Nuclear Respiratory Factor 1 (NRF-1) and Plays a Role in NRF-1 Transcriptional Regulation

Cited by 51 publications

References 38 publications

Poly(ADP-ribose) polymerases as modulators of mitochondrial activity

Poly(ADP-ribose) polymerases as modulators of mitochondrial activity

Signaling Mechanism of Poly(ADP-Ribose) Polymerase-1 (PARP-1) in Inflammatory Diseases

Activation of PARP-1 in response to bleomycin depends on the Ku antigen and protein phosphatase 5

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