ArticleNature communications2021
Chaperone-like protein DAY plays critical roles in photomorphogenesis.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Article
- The J-like domain CPP1-homolog CPL3 exclusively localizes in plastids and is not a key regulator of plant photomorphogenesis.Plant physiology · 2025Article
- Regulation of chloroplast biogenesis, development, and signaling by endogenous and exogenous cues.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024Review
- Genome-wide identification of DnaJ gene family inFrontiers in plant science · 2023Article
- J-like protein family of Arabidopsis thaliana: the enigmatic cousins of J-domain proteins.Plant cell reports · 2022Review
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Authors and funding
18 authors at 7 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photomorphogenesis, light-mediated development, is an essential feature of all terrestrial plants. While chloroplast development and brassinosteroid (BR) signaling are known players in photomorphogenesis, proteins that regulate both pathways have yet to be identified. Here we report that DE-ETIOLATION IN THE DARK AND YELLOWING IN THE LIGHT (DAY), a membrane protein containing DnaJ-like domain, plays a dual-role in photomorphogenesis by stabilizing the BR receptor, BRI1, as well as a key enzyme in chlorophyll biosynthesis, POR. DAY localizes to both the endomembrane and chloroplasts via its first transmembrane domain and chloroplast transit peptide, respectively, and interacts with BRI1 and POR in their respective subcellular compartments. Using genetic analysis, we show that DAY acts independently on BR signaling and chlorophyll biogenesis. Collectively, this work uncovers DAY as a factor that simultaneously regulates BR signaling and chloroplast development, revealing a key regulator of photomorphogenesis that acts across cell compartments.
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