ArticlePlant physiology2004
Patellin1, a novel Sec14-like protein, localizes to the cell plate and binds phosphoinositides.
Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 140 citations in OpenAlex.
- Molecular insights into the production of extracellular vesicles by plants.Plant physiology · 2026Article
- Genome-wide identification of the peanut PITP gene family and functional verification of AhSFH8 in resistance to Aspergillus flavus infection.BMC plant biology · 2025Article
- Sec14L6 is a phosphoinositide transporter that regulates phosphoinositide homeostasis and biogenesis of lipid droplets.Nature communications · 2025Article
- Locusts adopt IPScience advances · 2025Article
- Arabidopsis Produces Distinct Subpopulations of Extracellular Vesicles That Respond Differentially to Biotic Stress, Altering Growth and Infectivity of a Fungal Pathogen.Journal of extracellular vesicles · 2025Article
- Genome-wide identification of the Sec14 gene family and the response to salt and drought stress in soybean (Glycine max).BMC genomics · 2025Article
- OsSNDP4, a Sec14-nodulin Domain Protein, is Required for Pollen Development in Rice.Rice (New York, N.Y.) · 2024Article
- Article
- Methyl viologen-induced changes in the Arabidopsis proteome implicate PATELLIN 4 in oxidative stress responses.Journal of experimental botany · 2024Article
- Chloroplastic Sec14-like proteins modulate growth and phosphate deficiency responses in Arabidopsis and rice.Plant physiology · 2023Article
- SEC14-GOLD protein PATELLIN2 binds IRON-REGULATED TRANSPORTER1 linking root iron uptake to vitamin E.Plant physiology · 2023Article
- Role of SEC14-like phosphatidylinositol transfer proteins in membrane identity and dynamics.Frontiers in plant science · 2023Review
- Salt stress alters membrane lipid content and lipid biosynthesis pathways in the plasma membrane and tonoplast.Plant physiology · 2022Article
- Arabidopsis apoplastic fluid contains sRNA- and circular RNA-protein complexes that are located outside extracellular vesicles.The Plant cell · 2022Article
- ComparativeFrontiers in genetics · 2022Article
- Attracted to membranes: lipid-binding domains in plants.Plant physiology · 2021Article
- The AGCVIII kinase Dw2 modulates cell proliferation, endomembrane trafficking, and MLG/xylan cell wall localization in elongating stem internodes of Sorghum bicolor.The Plant journal : for cell and molecular biology · 2021Article
- YPIBP: A repository for phosphoinositide-binding proteins in yeast.Computational and structural biotechnology journal · 2021Article
- Phylogenetic analysis of plant multi-domain SEC14-like phosphatidylinositol transfer proteins and structure-function properties of PATELLIN2.Plant molecular biology · 2020Article
- A Sec14-like phosphatidylinositol transfer protein paralog defines a novel class of heme-binding proteins.eLife · 2020Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Membrane trafficking is central to construction of the cell plate during plant cytokinesis. Consequently, a detailed understanding of the process depends on the characterization of molecules that function in the formation, transport, targeting, and fusion of membrane vesicles to the developing plate, as well as those that participate in its consolidation and maturation into a fully functional partition. Here we report the initial biochemical and functional characterization of patellin1 (PATL1), a novel cell-plate-associated protein that is related in sequence to proteins involved in membrane trafficking in other eukaryotes. Analysis of the Arabidopsis genome indicated that PATL1 is one of a small family of Arabidopsis proteins, characterized by a variable N-terminal domain followed by two domains found in other membrane-trafficking proteins (Sec14 and Golgi dynamics domains). Results from immunolocalization and biochemical fractionation studies suggested that PATL1 is recruited from the cytoplasm to the expanding and maturing cell plate. In vesicle-binding assays, PATL1 bound to specific phosphoinositides, important regulators of membrane trafficking, with a preference for phosphatidylinositol(5)P, phosphatidylinositol(4,5)P(2), and phosphatidylinositol(3)P. Taken together, these findings suggest a role for PATL1 in membrane-trafficking events associated with cell-plate expansion or maturation and point to the involvement of phosphoinositides in cell-plate biogenesis.
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Registered trials
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