Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification and analysis of the interaction between Edc3 and Dcp2 in Saccharomyces cerevisiae.

Molecular and cellular biology - 1 Mar 2010

Harigaya Yuriko, Jones Brittnee N, Muhlrad Denise, Gross John D, Parker Roy

Abstract excerpt

Cap hydrolysis is a critical control point in the life of eukaryotic mRNAs and is catalyzed by the evolutionarily conserved Dcp1-Dcp2 complex. In Saccharomyces cerevisiae, decapping is modulated by several factors, including the Lsm family protein Edc3, which directly binds to Dcp2. We show that Edc3 binding to Dcp2 is mediated by a short peptide sequence located C terminal to the catalytic domain of Dcp2. This...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Conserved Sequence
Share to Endoribonucleases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ribosomal Proteins

Share to RNA-Binding Proteins

Share to RNA Precursors

Share to RNA Stability

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 20086104
DOI: 10.1128/MCB.01305-09
PMCID: PMC2832485

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and analysis of the interaction between Edc3 and Dcp2 in Saccharomyces cerevisiae.PMID 20086104Read ↗

Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae.Semantic proximity Read ↗

Control of mRNA decapping by positive and negative regulatory elements in the Dcp2 C-terminal domain.Semantic proximity Read ↗

A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting.Semantic proximity Read ↗

Targeted mRNA degradation by deadenylation-independent decapping.Semantic proximity Read ↗

New insights into the control of mRNA decapping.Semantic proximity Read ↗

Human DCP1 is crucial for mRNA decapping and possesses paralog-specific gene regulating functionsSemantic proximity Read ↗

The C-terminal region of Ge-1 presents conserved structural features required for P-body localization.Semantic proximity Read ↗

Arabidopsis DCP2, DCP1, and VARICOSE form a decapping complex required for postembryonic development.Semantic proximity Read ↗

Mutations in DCPS and EDC3 in autosomal recessive intellectual disability indicate a crucial role for mRNA decapping in neurodevelopment.Semantic proximity Read ↗

Decapping reaction of mRNA requires Dcp1 in fission yeast: its characterization in different species from yeast to human.Semantic proximity Read ↗

mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E.Semantic proximity Read ↗

The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.