ArticleNature plants2023
A new family of proteins is required for tethering of Casparian strip membrane domain and nutrient homoeostasis in rice.
Article in Nature plants, 2023. 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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10 citing papers in PubMed, 19 citations in OpenAlex.
- The GAPLESS-OsCASP complex mediates Casparian strip formation for proper localization and abundance of endodermal proteins in rice.Science advances · 2026Article
- Root structural remodeling under soil compaction for herbaceous plants.Plant diversity · 2026Article
- Dual roles of suberin deposition at the endodermal Casparian strip in manganese uptake of rice.Journal of experimental botany · 2025Article
- LD-transpeptidase-mediated cell envelope remodeling enables developmental transitions and survival inJournal of bacteriology · 2025Article
- Genome-Wide Identification of theInternational journal of molecular sciences · 2025Article
- Barriers and carriers for transition metal homeostasis in plants.Plant communications · 2025Review
- Root apoplastic barrier mechanism: an adaptive strategy to protect against salt stress.Molecular biology reports · 2024Review
- Exploring the function of plant root diffusion barriers in sealing and shielding for environmental adaptation.Nature plants · 2024Review
- An atlas of Brachypodium distachyon lateral root development.Biology open · 2024Article
- Salts out, water in.Nature plants · 2024Article
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11 authors at 2 institutions in 2 countries.
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Abstract
Cell-cell junctions are essential for multicellular organisms to maintain nutrient homoeostasis. A plant-type tight junction, the Casparian strip (CS)-Casparian strip membrane domain (CSD) that seals the paracellular space between adjacent endodermal cells, has been known for more than one hundred years. However, the molecular basis of this structure remains unknown. Here we report that a new family of proteins containing a glycine/alanine/proline-rich domain, a lectin domain and a secretory signal peptide (GAPLESS) mediates tethering of the plasma membrane to the CS in rice. The GAPLESS proteins are specifically localized in the CS of root endodermal cells, and loss of their functions results in a disabled cell-cell junction and disrupted nutrient homoeostasis. The GAPLESS protein forms a tight complex with OsCASP1 in the plasma membrane, thereby mediating the CS-CSD junction. This study provides valuable insights into the junctional complex of plant endodermal cells, shedding light on our understanding of nutrient homoeostasis in crops and the cell junctions of eukaryotes.
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