| MOV10 recruits DCP2 to decap human LINE-1 RNA by forming large cytoplasmic granules with phase separation properties. | MOV10 recruits DCP2 to decap human LINE-1 RNA by forming large cytoplasmic granules with phase separation properties.
Liu Q, Yi D, Ding J, Mao Y, Wang S, Ma L, Li Q, Wang J, Zhang Y, Zhao J, Guo S, Liu Z, Guo F, Zhao D, Liang C, Li X, Peng X, Cen S., Free PMC Article | 09/11/2023 |
| Intrinsically disordered regions of tristetraprolin and DCP2 directly interact to mediate decay of ARE-mRNA. | Intrinsically disordered regions of tristetraprolin and DCP2 directly interact to mediate decay of ARE-mRNA.
Maciej VD, Mateva N, Schwarz J, Dittmers T, Mallick M, Urlaub H, Chakrabarti S., Free PMC Article | 10/22/2022 |
| Human MARF1 is an endoribonuclease that interacts with the DCP1:DCP2 decapping complex and degrades target mRNAs. | Human MARF1 is an endoribonuclease that interacts with the DCP1:2 decapping complex and degrades target mRNAs.
Nishimura T, Fakim H, Brandmann T, Youn JY, Gingras AC, Jinek M, Fabian MR., Free PMC Article | 06/29/2019 |
| Human Dcp2 levels and activity are controlled by a competition between decapping complex assembly and Dcp2 degradation. | Competition between Decapping Complex Formation and Ubiquitin-Mediated Proteasomal Degradation Controls Human Dcp2 Decapping Activity.
Erickson SL, Corpuz EO, Maloy JP, Fillman C, Webb K, Bennett EJ, Lykke-Andersen J., Free PMC Article | 08/8/2015 |
| The data indicates that DCP2 activation by DCP1 occurs preferentially on the EDC4 scaffold, which may serve to couple DCP2 activation by DCP1 with 5'-to-3' mRNA degradation by XRN1 in human cells. | The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1.
Chang CT, Bercovich N, Loh B, Jonas S, Izaurralde E., Free PMC Article | 07/26/2014 |
| Data show that Y14 interacts directly with the decapping factor Dcp2 and the 5' cap structure of mRNAs via different but overlapping domains. | The RNA-binding protein Y14 inhibits mRNA decapping and modulates processing body formation.
Chuang TW, Chang WL, Lee KM, Tarn WY., Free PMC Article | 06/8/2013 |
| PNRC2 acts in synergy with Dcp1a to stimulate the decapping activity of Dcp2 by bridging the interaction between Dcp1a and Dcp2. | Structural basis of the PNRC2-mediated link between mrna surveillance and decapping.
Lai T, Cho H, Liu Z, Bowler MW, Piao S, Parker R, Kim YK, Song H. | 05/18/2013 |
| Like Dcp2, Nudt16 also regulates the stability of a subset of mRNAs including a member of the motin family of proteins involved in angiogenesis. | Multiple mRNA decapping enzymes in mammalian cells.
Song MG, Li Y, Kiledjian M., Free PMC Article | 01/1/2011 |
| These data support the novel notion of the association between Ro52 with hDCP2 protein in cytoplasmic p-bodies, playing a role in mRNA metabolism in response to cellular stimulation. | SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity.
Yamochi T, Ohnuma K, Hosono O, Tanaka H, Kanai Y, Morimoto C. | 01/21/2010 |
| hDcp2 can specifically bind to and can regulate the stability of a subset of mRNAs | Transcript-specific decapping and regulated stability by the human Dcp2 decapping protein.
Li Y, Song MG, Kiledjian M., Free PMC Article | 01/21/2010 |
| These data suggest that a human decapping complex containing decapping enzymes hDcp1a and hDcp2 may be recruited to mRNAs containing premature termination codons by the hUpf proteins. | Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay.
Lykke-Andersen J., Free PMC Article | 01/21/2010 |
| Human Dcp2 is a catalytically active mRNA decapping enzyme that localizes to the cytoplasm | 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., Free PMC Article | 01/21/2010 |
| an mRNA decapping enzyme demonstrated to contain intrinsic decapping activity | The hDcp2 protein is a mammalian mRNA decapping enzyme.
Wang Z, Jiao X, Carr-Schmid A, Kiledjian M., Free PMC Article | 01/21/2010 |
| LSm1-7 proteins colocalize with DCP1,DCP2 and Xrn1 in cytoplasmic foci | The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci.
Ingelfinger D, Arndt-Jovin DJ, Lührmann R, Achsel T., Free PMC Article | 01/21/2010 |