ArticleJournal of experimental botany2016
Arabidopsis SYT1 maintains stability of cortical endoplasmic reticulum networks and VAP27-1-enriched endoplasmic reticulum-plasma membrane contact sites.
Article in Journal of experimental botany, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 101 citations in OpenAlex.
- PERSPECTIVE: organelle positioning as a principle of metabolic regulation and stress tolerance.The Plant journal : for cell and molecular biology · 2026Review
- Alterations in the proteomic profiles of Arabidopsis roots triggered by sodium chloride stress are exacerbated by impaired function of SYNAPTOTAGMIN 1.BMC plant biology · 2025Article
- Concerted transport and phosphorylation of diacylglycerol at ER-PM contact sites regulate phospholipid dynamics during stress.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Extended Synaptotagmins ofPlants (Basel, Switzerland) · 2025Review
- The Wheat NLR Protein PM3b Localises to Endoplasmic Reticulum-Plasma Membrane Contact Sites and Interacts With AVRPM3Molecular plant pathology · 2025Article
- Functional and Structural Analysis Reveals Distinct Biological Roles of Plant Synaptotagmins in Response to Environmental Stress.Plant, cell & environment · 2025Article
- Lipid droplets in plants: turnover and stress responses.Frontiers in plant science · 2025Review
- ER-associated VAP27-1 and VAP27-3 proteins functionally link the lipid-binding ORP2A at the ER-chloroplast contact sites.Nature communications · 2024Article
- The VAMP-associated protein VAP27-1 plays a crucial role in plant resistance to ER stress by modulating ER-PM contact architecture in Arabidopsis.Plant communications · 2024Article
- A century journey of organelles research in the plant endomembrane system.The Plant cell · 2024Review
- Organelle Interactions in Plant Cells.Results and problems in cell differentiation · 2024Review
- SYNAPTOTAGMIN 4 is expressed mainly in the phloem and participates in abiotic stress tolerance in Arabidopsis.Frontiers in plant science · 2024Article
- Studying Plant ER-PM Contact Site Localized Proteins Using Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The plasma membrane - cell wall nexus in plant cells: focus on the Hechtian structure.Cell surface (Amsterdam, Netherlands) · 2023Review
- Protein interactomes for plant lipid biosynthesis and their biotechnological applications.Plant biotechnology journal · 2023Review
- Dynamic Regulation of Lipid Droplet Biogenesis in Plant Cells and Proteins Involved in the Process.International journal of molecular sciences · 2023Review
- The sieve-element endoplasmic reticulum: A focal point of phytoplasma-host plant interaction?Frontiers in microbiology · 2023Article
- Article
- Membrane contact sites and cytoskeleton-membrane interactions in autophagy.FEBS letters · 2022Review
- SEED LIPID DROPLET PROTEIN1, SEED LIPID DROPLET PROTEIN2, and LIPID DROPLET PLASMA MEMBRANE ADAPTOR mediate lipid droplet-plasma membrane tethering.The Plant cell · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Arabidopsis synaptotagmin 1 (SYT1) is localized on the endoplasmic reticulum-plasma membrane (ER-PM) contact sites in leaf and root cells. The ER-PM localization of Arabidopsis SYT1 resembles that of the extended synaptotagmins (E-SYTs) in animal cells. In mammals, E-SYTs have been shown to regulate calcium signaling, lipid transfer, and endocytosis. Arabidopsis SYT1 was reported to be essential for maintaining cell integrity and virus movement. This study provides detailed insight into the subcellular localization of SYT1 and VAP27-1, another ER-PM-tethering protein. SYT1 and VAP27-1 were shown to be localized on distinct ER-PM contact sites. The VAP27-1-enriched ER-PM contact sites (V-EPCSs) were always in contact with the SYT1-enriched ER-PM contact sites (S-EPCSs). The V-EPCSs still existed in the leaf epidermal cells of the SYT1 null mutant; however, they were less stable than those in the wild type. The polygonal networks of cortical ER disassembled and the mobility of VAP27-1 protein on the ER-PM contact sites increased in leaf cells of the SYT1 null mutant. These results suggest that SYT1 is responsible for stabilizing the ER network and V-EPCSs.
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