The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Reprogramming cellular events by poly(ADP-ribose)-binding proteins
Open accessAbstract
Poly(ADP-ribosyl)ation is a posttranslational modification catalyzed by the poly(ADP-ribose) polymerases (PARPs). These enzymes covalently modify glutamic, aspartic and lysine amino acid side chains of acceptor proteins by the sequential addition of ADP-ribose (ADPr) units. The poly(ADP-ribose) (pADPr) polymers formed alter the physico-chemical characteristics of the substrate with functional consequences on its biological activities. Recently, non-covalent binding to pADPr has emerged as a key mechanism to modulate and coordinate several intracellular pathways including the DNA damage response, protein stability and cell death. In this review, we describe the basis of non-covalent binding to pADPr that has led to the emerging concept of pADPr-responsive signaling pathways. This review emphasizes the structural elements and the modular strategies developed by pADPr-binding proteins to exert a fine-tuned control of a variety of pathways. Poly(ADP-ribosyl)ation reactions are highly regulated processes, both spatially and temporally, for which at least four specialized pADPr-binding modules accommodate different pADPr structures and reprogram protein functions. In this review, we highlight the role of well-characterized and newly discovered pADPr-binding modules in a diverse set of physiological functions.
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Cites
Systematic identification of genomic markers of drug sensitivity in cancer cells
Garnett, M. J., Edelman, E. J., Heidorn, S. J., Greenman, C. D., Dastur, A., Lau, K. W., Greninger, P., Thompson, I. R., Luo, X., Soares, J., et al. (2012) · Nature · doi:10.1038/nature11005 · Cited by 2,456
Mediation of Poly(ADP-Ribose) Polymerase-1-Dependent Cell Death by Apoptosis-Inducing Factor
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Self-citationChou, D. M., Adamson, B., Dephoure, N. E., Tan, X., Nottke, A. C., Hurov, K. E., Gygi, S. P., Colaiácovo, M. P., & Elledge, S. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012946107 · Cited by 529 · cited 1×
“Methyl-CpG-binding domain protein 2 (MBD2) has a GAR motif, while CHD4 (chromodomain helicase DNA binding protein 4) and MTA1 (metastasis associated 1) interact with pADPr through a still undefined motif (Chou et al., 2010; Lai and Wade, 2011; Polo et al., 2010).”
BackgroundAdamson, B., Smogorzewska, A., Sigoillot, F. D., King, R. W., & Elledge, S. J. (2012) · Nature Cell Biology · doi:10.1038/ncb2426 · Cited by 433
A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation
Timinszky, G., Till, S., Hassa, P. O., Hothorn, M., Kustatscher, G., Nijmeijer, B., Colombelli, J., Altmeyer, M., Stelzer, E. H. K., Scheffzek, K., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1664 · Cited by 416
Polo, S. E., Kaidi, A., Baskcomb, L., Galanty, Y., & Jackson, S. P. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.188 · Cited by 374
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Self-citationAndrabi, S. A., Kang, H. C., Haince, J.-F., Lee, Y.-I., Zhang, J., Chi, Z., West, A. B., Koehler, R. C., Poirier, G. G., Dawson, T. M., et al. (2011) · Nature Medicine · doi:10.1038/nm.2387 · Cited by 216
Self-citationThe histone variant macroH2A1.1 is recruited to DSBs through a mechanism involving PARP1
Xu, C., Xu, Y., Gursoy-Yuzugullu, O., & Price, B. D. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.09.030 · Cited by 71
Cited by
The multifaceted roles of PARP1 in DNA repair and chromatin remodelling
Ray Chaudhuri, A., & Nussenzweig, A. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.53 · Cited by 1,786
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Gupte, R., Liu, Z., & Kraus, W. L. (2017) · Genes & Development · doi:10.1101/gad.291518.116 · Cited by 681
“These ARBDs include PAR-bindingmotifs (PBMs), macrodomains, PAR-binding zinc finger (PBZ) modules, and WWE domains (Table 1; Kalisch et al. 2012; Barkauskaite et al. 2013; Karlberg et al. 2013; Krietsch et al. 2013).”
BackgroundParthanatos: mitochondrial‐linked mechanisms and therapeutic opportunities
Fatokun, A. A., Dawson, V. L., & Dawson, T. M. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12416 · Cited by 594
Self-citationMcGurk, L., Gomes, E., Guo, L., Mojsilovic-Petrovic, J., Tran, V., Kalb, R. G., Shorter, J., & Bonini, N. M. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.002 · Cited by 409
The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold
Knott, G. J., Bond, C. S., & Fox, A. H. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw271 · Cited by 326
Metadata
- Authors
- Krietsch, J., Rouleau, M., Pic, É., Ethier, C., Dawson, T. M., Dawson, V. L., Masson, J.-Y., Poirier, G. G., & Gagné, J.-P.
- Venue
- Molecular Aspects of Medicine
- Publisher
- Elsevier BV
- Published
- 2013-12
- Volume
- 34
- Issue
- 6
- Pages
- 1066-1087
- ISSN
- 0098-2997 (ISSN-L)
- OpenAlex
- W2083946902
- Cited by
- 169
- References
- 9
- FWCI
- 5.97
- Type
- journal article
- Language
- en
- Open access
- green
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- Krietsch, J., Rouleau, M., Pic, É., Ethier, C., Dawson, T. M., Dawson, V. L., Masson, J.-Y., Poirier, G. G., & Gagné, J.-P. (2013). Reprogramming cellular events by poly(ADP-ribose)-binding proteins. Molecular Aspects of Medicine. https://doi.org/10.1016/j.mam.2012.12.005
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