ArticlePlant & cell physiology2014
Significance of the photosystem II core phosphatase PBCP for plant viability and protein repair in thylakoid membranes.
Article in Plant & cell physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 45 citations in OpenAlex.
- Molecular architecture for state transition: insights from structural biology and evolutionary trajectories.Plant & cell physiology · 2025Review
- Structure, regulation and assembly of the photosynthetic electron transport chain.Nature reviews. Molecular cell biology · 2025Review
- Protein phosphorylation and oxidative protein modification promote plant photosystem II disassembly for repair.Plant communications · 2025Article
- Structural basis for an early stage of the photosystem II repair cycle in Chlamydomonas reinhardtii.Nature communications · 2024Article
- State Transition Regulation inPlant physiology · 2020Article
- Regulation of Light Harvesting inPlant physiology · 2020Article
- Thylakoid Protein Phosphorylation Dynamics in a Moss Mutant Lacking SERINE/THREONINE PROTEIN KINASE STN8.Plant physiology · 2019Article
- Phosphorylation of the Chloroplastic Metalloprotease FtsH inFrontiers in plant science · 2019Article
- Reduced Arogenate Dehydratase Expression: Ramifications for Photosynthesis and Metabolism.Plant physiology · 2018Article
- Loss of chloroplast-localized protein phosphatase 2Cs in Arabidopsis thaliana leads to enhancement of plant immunity and resistance to Xanthomonas campestris pv. campestris infection.Molecular plant pathology · 2018Article
- Protein Kinases and Phosphatases of the Plastid and Their Potential Role in Starch Metabolism.Frontiers in plant science · 2018Review
- Revisiting the photosystem II repair cycle.Plant signaling & behavior · 2016Review
- Downregulation of TAP38/PPH1 enables LHCII hyperphosphorylation in Arabidopsis mutant lacking LHCII docking site in PSI.FEBS letters · 2016Article
- Chloroplast immunophilins.Protoplasma · 2016Review
- Plants Actively Avoid State Transitions upon Changes in Light Intensity: Role of Light-Harvesting Complex II Protein Dephosphorylation in High Light.Plant physiology · 2015Article
- Compartmentalization of the protein repair machinery in photosynthetic membranes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Moderate Temperature Reduction Changes the High-Light Acclimation Strategy of Lettuce Plants.Physiologia plantarumArticle
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
PSII undergoes photodamage, which results in photoinhibition-the light-induced loss of photosynthetic activity. The main target of damage in PSII is the reaction center protein D1, which is buried in the massive 1.4 MDa PSII holocomplex. Plants have evolved a PSII repair cycle that degrades the damaged D1 subunit and replaces it with a newly synthesized copy. PSII core proteins, including D1, are phosphorylated in high light. This phosphorylation is important for the mobilization of photoinhibited PSII from stacked grana thylakoids to the repair machinery in distant unstacked stroma lamellae. It has been recognized that the degradation of the damaged D1 is more efficient after its dephosphorylation by a protein phosphatase. Recently a protein phosphatase 2C (PP2C)-type PSII core phosphatase (PBCP) has been discovered, which is involved in the dephosphorylation of PSII core proteins. Its role in PSII repair, however, is unknown. Using a range of spectroscopic and biochemical techniques, we report that the inactivation of the PBCP gene affects the growth characteristic of plants, with a decreased biomass and altered PSII functionality. PBCP mutants show increased phosphorylation of core subunits in dark and photoinhibitory conditions and a diminished degradation of the D1 subunit. Our results on D1 turnover in PBCP mutants suggest that dephosphorylation of PSII subunits is required for efficient D1 degradation.
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