| Dcp2 C-terminal cis-binding elements control selective targeting of the decapping enzyme by forming distinct decapping complexes. | Dcp2 C-terminal cis-binding elements control selective targeting of the decapping enzyme by forming distinct decapping complexes.
He F, Wu C, Jacobson A., Free PMC Article | 07/2/2022 |
| Suppressors of mRNA Decapping Defects Restore Growth Without Major Effects on mRNA Decay Rates or Abundance. | Suppressors of mRNA Decapping Defects Restore Growth Without Major Effects on mRNA Decay Rates or Abundance.
Kim M, van Hoof A., Free PMC Article | 07/17/2021 |
| Pby1 is a direct partner of the Dcp2 decapping enzyme. | Pby1 is a direct partner of the Dcp2 decapping enzyme.
Charenton C, Gaudon-Plesse C, Back R, Ulryck N, Cosson L, Séraphin B, Graille M., Free PMC Article | 09/12/2020 |
| results suggest that Scd6 can (i) recruit Dhh1 to confer translational repression and (ii) activate mRNA decapping by Dcp2 with attendant degradation of specific mRNAs in vivo, in a manner dependent on the Scd6 LSm domain and modulated by Ccr4 | Conserved mRNA-granule component Scd6 targets Dhh1 to repress translation initiation and activates Dcp2-mediated mRNA decay in vivo.
Zeidan Q, He F, Zhang F, Zhang H, Jacobson A, Hinnebusch AG., Free PMC Article | 03/9/2019 |
| Membrane-association of mRNA decapping factors, Dcp1, Dcp2, and Dhh1, is independent of stress in Saccharomyces cerevisiae. | Membrane-association of mRNA decapping factors is independent of stress in budding yeast.
Huch S, Gommlich J, Muppavarapu M, Beckham C, Nissan T., Free PMC Article | 02/17/2018 |
| This recruitment requires Hrr25 kinase activity and the Dcp2 decapping enzyme, a core constituent of these RNP granules. Interestingly, the data indicate that this localization sequesters active Hrr25 away from the remainder of the cytoplasm and thereby shields this enzyme from the degradation machinery during these periods of stress. | The Activity-Dependent Regulation of Protein Kinase Stability by the Localization to P-Bodies.
Zhang B, Shi Q, Varia SN, Xing S, Klett BM, Cook LA, Herman PK., Free PMC Article | 05/27/2017 |
| Results show that C-terminal domain of Dcp2 includes a set of conserved negative and positive regulatory elements reveal a pivotal role for the Dcp2 in mRNA decapping and lead to a new model for decapping enzyme regulation in vivo. | Control of mRNA decapping by positive and negative regulatory elements in the Dcp2 C-terminal domain.
He F, Jacobson A., Free PMC Article | 11/21/2015 |
| Local active site conformational changes are important for Dcp2 mRNA decapping activity. | Active site conformational dynamics are coupled to catalysis in the mRNA decapping enzyme Dcp2.
Aglietti RA, Floor SN, McClendon CL, Jacobson MP, Gross JD., Free PMC Article | 03/29/2014 |
| Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition | Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition.
Borja MS, Piotukh K, Freund C, Gross JD., Free PMC Article | 02/26/2011 |
| show using NMR that cap binds conserved residues on both the catalytic and regulatory domains of Dcp2. | A split active site couples cap recognition by Dcp2 to activation.
Floor SN, Jones BN, Hernandez GA, Gross JD., Free PMC Article | 10/4/2010 |
| Ste20 has an unexpected role in the modulation of mRNA decay and translation in Saccharomyces cerevisiae. Phosphorylation of Dcp2 by Ste20 is an important control point for mRNA decapping. | Dcp2 phosphorylation by Ste20 modulates stress granule assembly and mRNA decay in Saccharomyces cerevisiae.
Yoon JH, Choi EJ, Parker R., Free PMC Article | 07/26/2010 |
| These results raise a model for Dcp2 recruitment to specific mRNAs where regions outside the catalytic core promote the formation of different complexes involved in mRNA decapping. | Identification and analysis of the interaction between Edc3 and Dcp2 in Saccharomyces cerevisiae.
Harigaya Y, Jones BN, Muhlrad D, Gross JD, Parker R., Free PMC Article | 04/12/2010 |
| To understand regulation of Dcp2 by ligand interactions, we have assigned the backbone and sidechain methyl Ile (delta1), Leu and Val chemical shifts of the catalytic domain. | Backbone and sidechain methyl Ile (delta1), Leu and Val resonance assignments of the catalytic domain of the yeast mRNA decapping enzyme, Dcp2.
Deshmukh MV, Oku Y, Gross JD. | 01/21/2010 |