ADP-ribosylation Information & ADP-ribosylation Links at HealthHaven.com

ADP-ribosylation is a posttranslational modification of proteins that involves the addition of one or more ADP and ribose moieties.^[1]^[2] These reactions are involved in cell signaling and the control of many cell processes, including DNA repair and apoptosis.^[3]^[4]

[edit] ADP-ribosylation enzymes

This protein modification is produced by ADP-ribosyltransferase enzymes, which transfer the ADP-ribose group from nicotinamide adenine dinucleotide (NAD⁺) onto acceptors such as arginine, glutamic acid or aspartic acid residues in their substrate protein. In humans, one type of ADP-ribosyltransferases are the NAD:arginine ADP-ribosyltransferases, which modify amino acid residues in proteins such as histones by adding a single ADP-ribose group.^[5] These reactions are reversible; for example, when arginine is modified, the ADP-ribosylarginine produced can be removed by ADP-ribosylarginine hydrolases.^[6]

As well as the transfer of single ADP-ribose moieties, multiple groups can also be transferred to proteins to form long branched chains, in a reaction called poly(ADP-ribosyl)ation.^[7] This protein modification is carried out by the poly ADP-ribose polymerases (PARPs), which are found in most eukaryotes, but not prokaryotes or yeast.^[7]^[8] The poly(ADP-ribose) structure is involved in the regulation of several cellular events and is most important in the cell nucleus, in processes such as DNA repair and telomere maintenance.^[8]

[edit] Bacterial toxins

ADP-ribosylation is also responsible for the actions of some bacterial toxins, such as cholera toxin, diptheria toxin, and pertussis toxin. These toxin proteins are ADP-ribosyltransferases that modify target proteins in human cells. For example, cholera toxin ADP-ribosylates G proteins, which causes massive fluid secretion from the lining of the small intestine and results in life-threatening diarrhea.^[9]

[edit] See also

[edit] References

^ Belenky P, Bogan KL, Brenner C (2007). "NAD+ metabolism in health and disease". Trends Biochem. Sci. 32 (1): 12–9. doi:10.1016/j.tibs.2006.11.006. PMID 17161604. http://www.dartmouth.edu/~brenner/belenky07a.pdf.
^ Ziegler M (2000). "New functions of a long-known molecule. Emerging roles of NAD in cellular signaling". Eur. J. Biochem. 267 (6): 1550–64. doi:10.1046/j.1432-1327.2000.01187.x. PMID 10712584.
^ Berger F, Ramírez-Hernández MH, Ziegler M (2004). "The new life of a centenarian: signalling functions of NAD(P)". Trends Biochem. Sci. 29 (3): 111–8. doi:10.1016/j.tibs.2004.01.007. PMID 15003268.
^ Corda D, Di Girolamo M (2003). "Functional aspects of protein mono-ADP-ribosylation". EMBO J. 22 (9): 1953–8. doi:10.1093/emboj/cdg209. PMID 12727863. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=12727863.
^ Okazaki IJ, Moss J (1999). "Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases". Annual Review of Nutrition 19: 485–509. doi:10.1146/annurev.nutr.19.1.485. PMID 10448534.
^ Takada T, Okazaki IJ, Moss J (1994). "ADP-ribosylarginine hydrolases". Mol. Cell. Biochem. 138 (1-2): 119–22. doi:10.1007/BF00928452. PMID 7898453.
^ ^a ^b Diefenbach J, Bürkle A (2005). "Introduction to poly(ADP-ribose) metabolism". Cell. Mol. Life Sci. 62 (7-8): 721–30. doi:10.1007/s00018-004-4503-3. PMID 15868397.
^ ^a ^b Burkle A (2005). "Poly(ADP-ribose). The most elaborate metabolite of NAD+". FEBS J. 272 (18): 4576–89. doi:10.1111/j.1742-4658.2005.04864.x. PMID 16156780.
^ De Haan L, Hirst TR (2004). "Cholera toxin: a paradigm for multi-functional engagement of cellular mechanisms (Review)". Mol. Membr. Biol. 21 (2): 77–92. doi:10.1080/09687680410001663267. PMID 15204437.

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[0] Belenky P, Bogan KL, Brenner C (2007). "NAD+ metabolism in health and disease". Trends Biochem. Sci. 32 (1): 12–9. doi:10.1016/j.tibs.2006.11.006. PMID 17161604. http://www.dartmouth.edu/~brenner/belenky07a.pdf.

[1] Ziegler M (2000). "New functions of a long-known molecule. Emerging roles of NAD in cellular signaling". Eur. J. Biochem. 267 (6): 1550–64. doi:10.1046/j.1432-1327.2000.01187.x. PMID 10712584.

[2] Berger F, Ramírez-Hernández MH, Ziegler M (2004). "The new life of a centenarian: signalling functions of NAD(P)". Trends Biochem. Sci. 29 (3): 111–8. doi:10.1016/j.tibs.2004.01.007. PMID 15003268.

[3] Corda D, Di Girolamo M (2003). "Functional aspects of protein mono-ADP-ribosylation". EMBO J. 22 (9): 1953–8. doi:10.1093/emboj/cdg209. PMID 12727863. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=12727863.

[4] Okazaki IJ, Moss J (1999). "Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases". Annual Review of Nutrition 19: 485–509. doi:10.1146/annurev.nutr.19.1.485. PMID 10448534.

[5] Takada T, Okazaki IJ, Moss J (1994). "ADP-ribosylarginine hydrolases". Mol. Cell. Biochem. 138 (1-2): 119–22. doi:10.1007/BF00928452. PMID 7898453.

[Diefenbach-6] Diefenbach J, Bürkle A (2005). "Introduction to poly(ADP-ribose) metabolism". Cell. Mol. Life Sci. 62 (7-8): 721–30. doi:10.1007/s00018-004-4503-3. PMID 15868397.

[Burkle-7] Burkle A (2005). "Poly(ADP-ribose). The most elaborate metabolite of NAD+". FEBS J. 272 (18): 4576–89. doi:10.1111/j.1742-4658.2005.04864.x. PMID 16156780.

[8] De Haan L, Hirst TR (2004). "Cholera toxin: a paradigm for multi-functional engagement of cellular mechanisms (Review)". Mol. Membr. Biol. 21 (2): 77–92. doi:10.1080/09687680410001663267. PMID 15204437.

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Contents

[edit] ADP-ribosylation enzymes

[edit] Bacterial toxins

[edit] See also

[edit] References