ArticlePhysiologia plantarum2022
Chloroplast-localized PITP7 is essential for plant growth and photosynthetic function in Arabidopsis.
Article in Physiologia plantarum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Lipid metabolism and contact site homologs are present at the chloroplast envelope-thylakoid interface.Nature communications · 2026Article
- Genome-wide identification of the Sec14 gene family and the response to salt and drought stress in soybean (Glycine max).BMC genomics · 2025Article
- Structure, biogenesis, and evolution of thylakoid membranes.The Plant cell · 2024Review
- OsSNDP4, a Sec14-nodulin Domain Protein, is Required for Pollen Development in Rice.Rice (New York, N.Y.) · 2024Article
- Role of SEC14-like phosphatidylinositol transfer proteins in membrane identity and dynamics.Frontiers in plant science · 2023Review
- Chloroplast-localized PITP7 is essential for plant growth and photosynthetic function in Arabidopsis.Physiologia plantarum · 2022Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Recent studies of chloroplast-localized Sec14-like protein (CPSFL1, also known as phosphatidylinositol transfer protein 7, PITP7) showed that CPSFL1 is necessary for photoautotropic growth and chloroplast vesicle formation in Arabidopsis (Arabidopsis thaliana). Here, we investigated the functional roles of CPSFL1/PITP7 using two A. thaliana mutants carrying a putative null allele (pitp7-1) and a weak allele (pitp7-2), respectively. PITP7 transcripts were undetectable in pitp7-1 and less abundant in pitp7-2 than in the wild-type (WT). The severity of mutant phenotypes, such as plant developmental abnormalities, levels of plastoquinone-9 (PQ-9) and chlorophylls, photosynthetic protein complexes, and photosynthetic performance, were well related to PITP7 transcript levels. The pitp7-1 mutation was seedling lethal and was associated with significantly lower levels of PQ-9 and major photosynthetic proteins. pitp7-2 plants showed greater susceptibility to high-intensity light stress than the WT, attributable to defects in nonphotochemical quenching and photosynthetic electron transport. PITP7 is specifically bound to phosphatidylinositol phosphates (PIPs) in lipid-binding assays in vitro, and the point mutations R82, H125, E162, or K233 reduced the binding affinity of PITP7 to PIPs. Further, constitutive expression of PITP7
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