ArticleThe Plant journal : for cell and molecular biology2019
Light-dependent N-terminal phosphorylation of LHCSR3 and LHCB4 are interlinked in Chlamydomonas reinhardtii.
Article in The Plant journal : for cell and molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Roles of LHCSR3 and STT7 in the remodeling of thylakoid supercomplexes in Chlamydomonas reinhardtii under UV-B treatment.The New phytologist · 2026Article
- Quantitative phosphoproteomics profiling reveals the regulatory mechanisms underlying high light stress in maize and rice.Photosynthesis research · 2026Article
- The amino terminus of PetD is essential for cytochrome bNature plants · 2026Article
- Macroscale structural changes of thylakoid architecture during high light acclimation in Chlamydomonas reinhardtii.Photosynthesis research · 2024Article
- NovoLign: metaproteomics by sequence alignment.ISME communications · 2024Article
- Widening the landscape of transcriptional regulation of green algal photoprotection.Nature communications · 2023Article
- Light-independent regulation of algal photoprotection by CONature communications · 2023Article
- Remodeling of algal photosystem I through phosphorylation.Bioscience reports · 2023Article
- Juggling Lightning: How Chlorella ohadii handles extreme energy inputs without damage.Photosynthesis research · 2021Article
- Photosystem II antenna complexes CP26 and CP29 are essential for nonphotochemical quenching in Chlamydomonas reinhardtii.Plant, cell & environment · 2020Article
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Authors and funding
6 authors.
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Abstract
Phosphorylation dynamics of LHCSR3 were investigated in Chlamydomonas reinhardtii by quantitative proteomics and genetic engineering. LHCSR3 protein expression and phosphorylation were induced in high light. Our data revealed synergistic and dynamic N-terminal LHCSR3 phosphorylation. Phosphorylated and nonphosphorylated LHCSR3 associated with PSII-LHCII supercomplexes. The phosphorylation status of LHCB4 was closely linked to the phosphorylation of multiple sites at the N-terminus of LHCSR3, indicating that LHCSR3 phosphorylation may operate as a molecular switch modulating LHCB4 phosphorylation, which in turn is important for PSII-LHCII disassembly. Notably, LHCSR3 phosphorylation diminished under prolonged high light, which coincided with onset of CEF. Hierarchical clustering of significantly altered proteins revealed similar expression profiles of LHCSR3, CRX, and FNR. This finding indicated the existence of a functional link between LHCSR3 protein abundance and phosphorylation, photosynthetic electron flow, and the oxidative stress response.
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