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

The phosphorylation of carboxyl-terminal eIF2α by SPA kinases contributes to enhanced translation efficiency during photomorphogenesis.

Nature communications - 24 Apr 2024

Chang Hui-Hsien, Huang Lin-Chen, Browning Karen S, Huq Enamul, Cheng Mei-Chun

Abstract excerpt

Light triggers an enhancement of global translation during photomorphogenesis in Arabidopsis, but little is known about the underlying mechanisms. The phosphorylation of the α-subunit of eukaryotic initiation factor 2 (eIF2α) at a conserved serine residue in the N-terminus has been shown as an important mechanism for the regulation of protein synthesis in mammalian and yeast cells. However, whether the...

Read the complete abstract on PubMed

Topics

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

Share to Arabidopsis Proteins
Share to Cell Cycle Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Eukaryotic Initiation Factor-2

Share to Gene Expression Regulation, Plant

Share to Phosphorylation

Share to Protein Biosynthesis

Share to Protein Serine-Threonine Kinases

Source

Open in PubMed Open full text

Identifiers

PMID: 38658612
DOI: 10.1038/s41467-024-47848-7
PMCID: PMC11043401

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The phosphorylation of carboxyl-terminal eIF2α by SPA kinases contributes to enhanced translation efficiency during photomorphogenesis.PMID 38658612Read ↗

Arabidopsis phytochrome B promotes SPA1 nuclear accumulation to repress photomorphogenesis under far-red light.Semantic proximity Read ↗

Fully Tunable Phosphorylation of RPS6A Ensures the Successful Development of Arabidopsis Seedlings.Semantic proximity Read ↗

Arabidopsis COP1 and SPA genes are essential for plant elongation but not for acceleration of flowering time in response to a low red light to far-red light ratio.Semantic proximity Read ↗

Eukaryotic initiation factor 6, an evolutionarily conserved regulator of ribosome biogenesis and protein translation.Semantic proximity Read ↗

The SPA1-like proteins SPA3 and SPA4 repress photomorphogenesis in the light.Semantic proximity Read ↗

The SPA quartet: a family of WD-repeat proteins with a central role in suppression of photomorphogenesis in arabidopsis.Semantic proximity Read ↗

The Arabidopsis SPA1 gene is required for circadian clock function and photoperiodic flowering.Semantic proximity Read ↗

Mutations in the N-terminal kinase-like domain of the repressor of photomorphogenesis SPA1 severely impair SPA1 function but not light responsiveness in Arabidopsis.Semantic proximity Read ↗

Translation initiation factor AteIF(iso)4E is involved in selective mRNA translation in Arabidopsis thaliana seedlings.Semantic proximity Read ↗

CpLEPA is critical for chloroplast protein synthesis under suboptimal conditions in Arabidopsis thaliana.Semantic proximity Read ↗

Functional analysis of COP1 and SPA orthologs from Physcomitrella and rice during photomorphogenesis of transgenic Arabidopsis reveals distinct evolutionary conservation.Semantic proximity Read ↗

High light-dependent phosphorylation of photosystem II inner antenna CP29 in monocots is STN7 independent and enhances nonphotochemical quenching.Semantic proximity Read ↗

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