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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

DCP2  -  decapping mRNA 2

Homo sapiens

Synonyms: NUDT20, Nucleoside diphosphate-linked moiety X motif 20, Nudix motif 20, hDpc, m7GpppN-mRNA hydrolase, ...
 
 
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High impact information on DCP2

  • We have cloned cDNAs for the human homologues of the yeast Dcp1 and Dcp2 factors involved in the major (5'-3') and NMD mRNA decay pathways [1].
  • Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures [1].
  • Oligonucleotides capped with m(2)(7,3'-O)Gpp(CH2)pG were resistant to hydrolysis by recombinant human Dcp2 in vitro. mRNAs capped with m(2)(7,3'-O)Gpp(CH2)pG, but not m(2)(7,3'-O)Gp(CH2)ppG, were more stable in vivo, indicating that the 5'-->3' pathway makes a major contribution to overall degradation [2].
  • To test the relative contributions of the 5'-->3' versus 3'-->5' pathways, we designed and synthesized two new cap analogs, in which a methylene group was substituted between the alpha- and beta-phosphate moieties, m(2)(7,3'-O)Gpp(CH2)pG and m(2)(7,3'-O)Gp(CH2)ppG, that are predicted to be resistant to cleavage by Dcp1/Dcp2 and DcpS, respectively [2].
  • Ge-1 co-localized with previously identified P-body components, including proteins involved in mRNA decapping (DCP1a and DCP2) and the autoantigen GW 182 [3].
 

Biological context of DCP2

  • Consistent with their role in mRNA decay, DCP1, DCP2, and VCS colocalize in cytoplasmic foci, which are putative Arabidopsis processing bodies [4].
 

Associations of DCP2 with chemical compounds

  • A major product of DCPP, Disease Control Priorities in Developing Countries, 2nd edition (DCP2), focuses on the assessment of the cost-effectiveness of health-improving strategies (or interventions) for the conditions responsible for the greatest burden of disease [5].
  • The Dcp2 decapping enzyme utilizes capped mRNA as substrate and hydrolyses the cap to release m(7)GDP (N7-methyl GDP), while a scavenger decapping enzyme, DcpS, utilizes cap dinucleotides or capped oligonucleotides as substrate and releases m(7)GMP (N7-methyl GMP) [6].
 

Other interactions of DCP2

  • Decapping of messenger RNA was thought to involve a complex of only Dcp1 and Dcp2, but new data suggest that a larger multisubunit decapping complex exists in mammals [7].

References

  1. Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. van Dijk, E., Cougot, N., Meyer, S., Babajko, S., Wahle, E., Séraphin, B. EMBO J. (2002) [Pubmed]
  2. Differential inhibition of mRNA degradation pathways by novel cap analogs. Grudzien, E., Kalek, M., Jemielity, J., Darzynkiewicz, E., Rhoads, R.E. J. Biol. Chem. (2006) [Pubmed]
  3. Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body. Yu, J.H., Yang, W.H., Gulick, T., Bloch, K.D., Bloch, D.B. RNA (2005) [Pubmed]
  4. Arabidopsis DCP2, DCP1, and VARICOSE Form a Decapping Complex Required for Postembryonic Development. Xu, J., Yang, J.Y., Niu, Q.W., Chua, N.H. Plant Cell (2006) [Pubmed]
  5. Advancement of global health: key messages from the Disease Control Priorities Project. Laxminarayan, R., Mills, A.J., Breman, J.G., Measham, A.R., Alleyne, G., Claeson, M., Jha, P., Musgrove, P., Chow, J., Shahid-Salles, S., Jamison, D.T. Lancet (2006) [Pubmed]
  6. Decapping the message: a beginning or an end. Liu, H., Kiledjian, M. Biochem. Soc. Trans. (2006) [Pubmed]
  7. More than 1 + 2 in mRNA decapping. Bail, S., Kiledjian, M. Nat. Struct. Mol. Biol. (2006) [Pubmed]
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