Difference between revisions of "ADP-ribosylation"

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[[Image:Adenosine diphosphate ribose.svg|thumb|250px|[[Adenosine diphosphate ribose|ADP ribose]]]]
 
[[Image:Adenosine diphosphate ribose.svg|thumb|250px|[[Adenosine diphosphate ribose|ADP ribose]]]]
'''ADP-ribosylation''' is a [[posttranslational modification]] of [[protein]]s that involves the addition of one or more [[ADP]] and [[ribose]] moieties.<ref>{{cite journal |author=Belenky P, Bogan KL, Brenner C |title=NAD+ metabolism in health and disease |journal=Trends Biochem. Sci. |volume=32 |issue=1 |pages=12-9 |year=2007 |pmid=17161604 |url=http://www.dartmouth.edu/~brenner/belenky07a.pdf}}</ref><ref>{{cite journal |author=Ziegler M |title=New functions of a long-known molecule. Emerging roles of NAD in cellular signaling |journal=Eur. J. Biochem. |volume=267 |issue=6 |pages=1550-64 |year=2000 |pmid=10712584}}</ref> These reactions are involved in [[cell signaling]] and the control of many cell processes, including [[DNA repair]] and [[apoptosis]].<ref>{{cite journal |author=Berger F, Ramírez-Hernández MH, Ziegler M |title=The new life of a centenarian: signalling functions of NAD(P) |journal=Trends Biochem. Sci. |volume=29 |issue=3 |pages=111-8 |year=2004 |pmid=15003268}}</ref>  
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'''ADP-ribosylation''' is a [[posttranslational modification]] of [[protein]]s that involves the addition of one or more [[ADP]] and [[ribose]] moieties.<ref>{{cite journal |author=Belenky P, Bogan KL, Brenner C |title=NAD+ metabolism in health and disease |journal=Trends Biochem. Sci. |volume=32 |issue=1 |pages=12-9 |year=2007 |pmid=17161604 |url=http://www.dartmouth.edu/~brenner/belenky07a.pdf}}</ref><ref>{{cite journal |author=Ziegler M |title=New functions of a long-known molecule. Emerging roles of NAD in cellular signaling |journal=Eur. J. Biochem. |volume=267 |issue=6 |pages=1550-64 |year=2000 |pmid=10712584}}</ref> These reactions are involved in [[cell signaling]] and the control of many cell processes, including [[DNA repair]] and [[apoptosis]].<ref>{{cite journal |author=Berger F, Ramírez-Hernández MH, Ziegler M |title=The new life of a centenarian: signalling functions of NAD(P) |journal=Trends Biochem. Sci. |volume=29 |issue=3 |pages=111-8 |year=2004 |pmid=15003268}}</ref><ref>{{cite journal |author=Corda D, Di Girolamo M |title=Functional aspects of protein mono-ADP-ribosylation |journal=EMBO J. |volume=22 |issue=9 |pages=1953–8 |year=2003 |pmid=12727863 |url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=12727863}}</ref>
  
 
==ADP-ribosylation enzymes==
 
==ADP-ribosylation enzymes==
This protein modification is produced by [[ADP-ribosyltransferase]] enzymes, which transfer the ADP-ribose group from [[nicotinamide adenine dinucleotide]] (NAD<sup>+</sup>) onto acceptors such as [[arginine]], [[glutamic acid]] or [[aspartic acid]] residues in their substrate protein. In [[human]]s, one type of ADP-ribosyltransferases are the NAD:arginine ADP-ribosyltransferases, which modify amino acid residues in proteins such as [[histone]]s by adding a single ADP-ribose group.<ref>{{cite journal |author=Okazaki IJ, Moss J |title=Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases |journal=Annu. Rev. Nutr. |volume=19 |issue= |pages=485-509 |year=1999 |pmid=10448534}}</ref> These reactions are reversible; for example, when arginine is modified, the ADP-ribosylarginine produced can be removed by ADP-ribosylarginine hydrolases.<ref>{{cite journal |author=Takada T, Okazaki IJ, Moss J |title=ADP-ribosylarginine hydrolases |journal=Mol. Cell. Biochem. |volume=138 |issue=1-2 |pages=119-22 |year=1994 |pmid=7898453}}</ref>
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This protein modification is produced by [[ADP-ribosyltransferase]] enzymes, which transfer the ADP-ribose group from [[nicotinamide adenine dinucleotide]] (NAD<sup>+</sup>) onto acceptors such as [[arginine]], [[glutamic acid]] or [[aspartic acid]] residues in their substrate protein. In [[human]]s, one type of ADP-ribosyltransferases are the NAD:arginine ADP-ribosyltransferases, which modify amino acid residues in proteins such as [[histone]]s by adding a single ADP-ribose group.<ref>{{cite journal |author=Okazaki IJ, Moss J |title=Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases |journal=Annual Review of Nutrition |volume=19 |pages=485-509 |year=1999 |pmid=10448534 }}</ref> These reactions are reversible; for example, when arginine is modified, the ADP-ribosylarginine produced can be removed by ADP-ribosylarginine hydrolases.<ref>{{cite journal |author=Takada T, Okazaki IJ, Moss J |title=ADP-ribosylarginine hydrolases |journal=Mol. Cell. Biochem. |volume=138 |issue=1-2 |pages=119-22 |year=1994 |pmid=7898453 }}</ref>
  
 
ADP-ribose can also be transferred to proteins in long branched chains, in a reaction called poly(ADP-ribosyl)ation.<ref name=Diefenbach>{{cite journal |author=Diefenbach J, Bürkle A |title=Introduction to poly(ADP-ribose) metabolism |journal=Cell. Mol. Life Sci. |volume=62 |issue=7-8 |pages=721-30 |year=2005 |pmid=15868397}}</ref> This protein modification is carried out by the [[Poly ADP ribose polymerase|poly ADP-ribose polymerase]]s (PARPs) which are found in most [[eukaryote]]s, but not [[prokaryote]]s or [[yeast]].<ref name=Diefenbach/><ref name=Burkle>{{cite journal |author=Burkle A |title=Poly(ADP-ribose). The most elaborate metabolite of NAD+ |journal=FEBS J. |volume=272 |issue=18 |pages=4576-89 |year=2005 |pmid=16156780}}</ref> 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.<ref name=Burkle/>
 
ADP-ribose can also be transferred to proteins in long branched chains, in a reaction called poly(ADP-ribosyl)ation.<ref name=Diefenbach>{{cite journal |author=Diefenbach J, Bürkle A |title=Introduction to poly(ADP-ribose) metabolism |journal=Cell. Mol. Life Sci. |volume=62 |issue=7-8 |pages=721-30 |year=2005 |pmid=15868397}}</ref> This protein modification is carried out by the [[Poly ADP ribose polymerase|poly ADP-ribose polymerase]]s (PARPs) which are found in most [[eukaryote]]s, but not [[prokaryote]]s or [[yeast]].<ref name=Diefenbach/><ref name=Burkle>{{cite journal |author=Burkle A |title=Poly(ADP-ribose). The most elaborate metabolite of NAD+ |journal=FEBS J. |volume=272 |issue=18 |pages=4576-89 |year=2005 |pmid=16156780}}</ref> 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.<ref name=Burkle/>
  
 
==Bacterial toxins==
 
==Bacterial toxins==
ADP-ribosylation is also responsible for the actions of several bacterial [[toxin]]s, such as [[cholera toxin]] and [[pertussis toxin]]. These toxin proteins are ADP-ribosyltransferases that modify target proteins in human cells. For example, cholera toxin ADP-ribosylates [[G protein]]s, which causes massive fluid secretion from the lining of the small intestine and results in life-threatening [[diarrhea]].<ref>{{cite journal |author=De Haan L, Hirst TR |title=Cholera toxin: a paradigm for multi-functional engagement of cellular mechanisms (Review) |journal=Mol. Membr. Biol. |volume=21 |issue=2 |pages=77-92 |year=2004 |pmid=15204437}}</ref>
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ADP-ribosylation is also responsible for the actions of some bacterial [[toxin]]s, such as [[cholera toxin]] and [[pertussis toxin]]. These toxin proteins are ADP-ribosyltransferases that modify target proteins in human cells. For example, cholera toxin ADP-ribosylates [[G protein]]s, which causes massive fluid secretion from the lining of the small intestine and results in life-threatening [[diarrhea]].<ref>{{cite journal |author=De Haan L, Hirst TR |title=Cholera toxin: a paradigm for multi-functional engagement of cellular mechanisms (Review) |journal=Mol. Membr. Biol. |volume=21 |issue=2 |pages=77-92 |year=2004 |pmid=15204437}}</ref>
  
 
==See also==
 
==See also==
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==References==
 
==References==
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{{Protein posttranslational modification}}
  
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[[Category:Signal transduction]]
 
[[Category:Signal transduction]]
 
[[Category:Posttranslational modification]]
 
[[Category:Posttranslational modification]]
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[[ja:ADPリボース化反応]]

Revision as of 17:08, 8 December 2007

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]

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]

ADP-ribose can also be transferred to proteins in 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]

Bacterial toxins

ADP-ribosylation is also responsible for the actions of some bacterial toxins, such as cholera 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]

See also

References

  1. Belenky P, Bogan KL, Brenner C (2007). "NAD+ metabolism in health and disease" (PDF). Trends Biochem. Sci. 32 (1): 12–9. PMID 17161604.
  2. Ziegler M (2000). "New functions of a long-known molecule. Emerging roles of NAD in cellular signaling". Eur. J. Biochem. 267 (6): 1550–64. PMID 10712584.
  3. 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. PMID 15003268.
  4. Corda D, Di Girolamo M (2003). "Functional aspects of protein mono-ADP-ribosylation". EMBO J. 22 (9): 1953–8. PMID 12727863.
  5. Okazaki IJ, Moss J (1999). "Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases". Annual Review of Nutrition. 19: 485–509. PMID 10448534.
  6. Takada T, Okazaki IJ, Moss J (1994). "ADP-ribosylarginine hydrolases". Mol. Cell. Biochem. 138 (1–2): 119–22. PMID 7898453.
  7. 7.0 7.1 Diefenbach J, Bürkle A (2005). "Introduction to poly(ADP-ribose) metabolism". Cell. Mol. Life Sci. 62 (7–8): 721–30. PMID 15868397.
  8. 8.0 8.1 Burkle A (2005). "Poly(ADP-ribose). The most elaborate metabolite of NAD+". FEBS J. 272 (18): 4576–89. PMID 16156780.
  9. 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. PMID 15204437.



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