The macro domain is an ADP-ribose binding module

Karras, Georgios I.; Kustatscher, Georg; Buhecha, Heeran R.; Allen, Mark D.; Pugieux, Céline; Sait, Fiona; Bycroft, Mark; Ladurner, Andreas G.

doi:10.1038/sj.emboj.7600664

Cited by 449 publications

(533 citation statements)

References 69 publications

(76 reference statements)

Supporting

Mentioning

504

Contrasting

Unclassified

Order By: Relevance

“…Unlike PARP1, PARP14 appears to catalyze mono-and not poly-ADP ribosylation (29). Furthermore, PARP14 is one of three members of the BAL family of PARPs containing macrodomains ("macro-PARPs") that bind (poly-)ADP ribose (32,33). PARP1's roles in DNA repair, chromatin, and inflammation have been identified (30,31), but the physiological functions of monotransferase or macro-PARP family members are not known.…”

Section: Discussionmentioning

confidence: 99%

Glycolytic rate and lymphomagenesis depend on PARP14, an ADP ribosyltransferase of the B aggressive lymphoma (BAL) family

Cho¹,

Ahn²,

Bhargava

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

128

View full text Add to dashboard Cite

Poly(ADP-ribose)polymerase (PARP)14-a member of the B aggressive lymphoma (BAL) family of macrodomain-containing PARPs-is an ADP ribosyltransferase that interacts with Stat6, enhances induction of certain genes by IL-4, and is expressed in B lymphocytes. We now show that IL-4 enhancement of glycolysis in B cells requires PARP14 and that this process is central to a role of PARP14 in IL-4-induced survival. Thus, enhancements of AMP-activated protein kinase activity restored both IL-4-induced glycolytic activity in Parp14 −/− B cells and prosurvival signaling by this cytokine. Suppression of apoptosis is central to B-lymphoid oncogenesis, and elevated macro-PARP expression has been correlated with lymphoma aggressiveness. Strikingly, PARP14 deficiency delayed B lymphomagenesis and reversed the block to B-cell maturation driven by the Myc oncogene. Collectively, these findings reveal links between a mammalian ADP ribosyltransferase, cytokine-regulated metabolic activity, and apoptosis; show that PARP14 influences Myc-induced oncogenesis; and suggest that the PARP14-dependent capacity to increase cellular metabolic rates may be an important determinant of lymphoma pathobiology.

show abstract

Section: Discussionmentioning

confidence: 99%

Glycolytic rate and lymphomagenesis depend on PARP14, an ADP ribosyltransferase of the B aggressive lymphoma (BAL) family

Cho¹,

Ahn²,

Bhargava

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

128

View full text Add to dashboard Cite

show abstract

“…Interestingly, this domain is able to negatively regulate PARP-1 activity on particular promoters that must remain inactive in the absence of appropriated stimulation or on the inactive X chromosome (Ouararhni et al, 2006;Nusinow et al, 2007). Macro domains were recently shown to bind ADP-ribose and its derivatives (Karras et al, 2005). Those of PARP-9 and of some RNA virus encoding nonstructural proteins (from the Severe Acute Respiratory Syndrome Coronavirus SARS-CoV, the hepatitis E virus, and the Semliki Forest virus) are indeed able to bind poly(ADP-ribose) (Karras et al, 2005;Egloff et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…Macro domains were recently shown to bind ADP-ribose and its derivatives (Karras et al, 2005). Those of PARP-9 and of some RNA virus encoding nonstructural proteins (from the Severe Acute Respiratory Syndrome Coronavirus SARS-CoV, the hepatitis E virus, and the Semliki Forest virus) are indeed able to bind poly(ADP-ribose) (Karras et al, 2005;Egloff et al, 2006). PARP-9 (also called BAL1, B-aggressive lymphoma 1) was identified according to its differential expression in diffuse large B cell lymphomas (DL-BCL), higher in some chemoresistant tumors with poor prognosis, particularly those associating a brisk host inflammatory response due to tumour infiltration by T lymphocytes and dendritic cells (Aguiar et al, 2000;Juszczynski et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

The macroPARP genes parp‐9 and parp‐14 are developmentally and differentially regulated in mouse tissues

Hakmé

Huber

Dollé

et al. 2007

Developmental Dynamics

View full text Add to dashboard Cite

The macroPARPs Parp-9 and Parp-14 are macro domain containing poly(ADP-ribose) polymerases involved in transcriptional regulation in response to immunoregulatory cytokines. Their genes reside in the same locus (16B3), and the Parp-9 gene lies head-to-head and shares its promoter with the gene encoding its partner, Bbap. Here, we provide a detailed analysis of Parp-9, Parp-14, and Bbap expression during mouse development and adulthood. Parp-9 is developmentally regulated, and prominently expressed in the thymus and specific regions of the brain and gut. In adults, highest expression is maintained in the thymus and intestine. Parp-14 is more weakly expressed, mainly in the thymus during development and in adulthood. In addition, we show that Bbap is essentially coexpressed with Parp-9 during development and in adult mouse. However, the different levels of their transcripts detected in the developing brain and gut suggest that Bbap and Parp-9 display both common and independent tissue-specific regulations.

show abstract

“…Using isothermal titration calorimetry (ITC) assays, we measured the affinity between PAR and these FHA/ BRCT domains (Fig. 1C), which is in the physiologically relevant range and is similar to that between PAR and other PAR-binding domains (Karras et al 2005;Wang et al 2012). Since PAR is the ADP-ribose polymer with mixed length and contains both linear and branched forms, the affinity between the PAR-binding domain and PAR could not be accurately measured.…”

Section: A Set Of Brct and Fha Domains Binds Parmentioning

confidence: 99%

“…Recently, several PAR-binding proteins have been identified as the ''readers'' to recognize PAR signals (Karras et al 2005;Ahel et al 2008;Wang et al 2012), suggesting that PAR is likely to function as recruiting signals to induce DNA damage response factors to DNA damage sites. To identify other PAR-binding modules, we examined both the Forkhead-associated (FHA) domain and the BRCA1 C-terminal (BRCT) domain.…”

mentioning

confidence: 99%

The FHA and BRCT domains recognize ADP-ribosylation during DNA damage response

et al. 2013

View full text Add to dashboard Cite

Poly-ADP-ribosylation is a unique post-translational modification participating in many biological processes, such as DNA damage response. Here, we demonstrate that a set of Forkhead-associated (FHA) and BRCA1 C-terminal (BRCT) domains recognizes poly(ADP-ribose) (PAR) both in vitro and in vivo. Among these FHA and BRCT domains, the FHA domains of APTX and PNKP interact with iso-ADP-ribose, the linkage of PAR, whereas the BRCT domains of Ligase4, XRCC1, and NBS1 recognize ADP-ribose, the basic unit of PAR. The interactions between PAR and the FHA or BRCT domains mediate the relocation of these domain-containing proteins to DNA damage sites and facilitate the DNA damage response. Moreover, the interaction between PAR and the NBS1 BRCT domain is important for the early activation of ATM during DNA damage response and ATM-dependent cell cycle checkpoint activation. Taken together, our results demonstrate two novel PAR-binding modules that play important roles in DNA damage response.

show abstract

The macro domain is an ADP-ribose binding module

Cited by 449 publications

References 69 publications

Glycolytic rate and lymphomagenesis depend on PARP14, an ADP ribosyltransferase of the B aggressive lymphoma (BAL) family

Glycolytic rate and lymphomagenesis depend on PARP14, an ADP ribosyltransferase of the B aggressive lymphoma (BAL) family

The macroPARP genes parp‐9 and parp‐14 are developmentally and differentially regulated in mouse tissues

The FHA and BRCT domains recognize ADP-ribosylation during DNA damage response

Contact Info

Product

Resources

About