ArticleMolecular & cellular proteomics : MCP2019
Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain.
Article in Molecular & cellular proteomics : MCP, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 34 citations in OpenAlex.
- Unconventional vesicle transport driven by formin-actin-myosin working system during pollen germination.Science advances · 2026Article
- Transcriptional and post-translational regulation of aquaporins in plants.Stress biology · 2026Review
- Integration of high-throughput proteomic data and complementary omics layers with PriOmics.Genome research · 2026Article
- The conserved AvrE family of bacterial effectors: functions and targets during pathogenesis.Trends in microbiology · 2025Review
- The leucine-rich repeat receptor kinase QSK1 regulates PRR-RBOHD complexes targeted by the bacterial effector HopF2Pto.The Plant cell · 2024Article
- Phosphoregulation in the N-terminus of NRT2.1 affects nitrate uptake by controlling the interaction of NRT2.1 with NAR2.1 and kinase HPCAL1 in Arabidopsis.Journal of experimental botany · 2024Article
- DeepFLR facilitates false localization rate control in phosphoproteomics.Nature communications · 2023Article
- Spatial proteomics of vesicular trafficking: coupling mass spectrometry and imaging approaches in membrane biology.Plant biotechnology journal · 2023Review
- The mycorrhiza-specific ammonium transporter ZmAMT3;1 mediates mycorrhiza-dependent nitrogen uptake in maize roots.The Plant cell · 2022Article
- Hormonal and environmental signaling pathways target membrane water transport.Plant physiology · 2021Review
- Cell Wall Invertase Is Essential for Ovule Development through Sugar Signaling Rather Than Provision of Carbon Nutrients.Plant physiology · 2020Article
- Plasma Membrane-Associated Receptor-like Kinases Relocalize to Plasmodesmata in Response to Osmotic Stress.Plant physiology · 2019Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sucrose as a product of photosynthesis is the major carbohydrate translocated from photosynthetic leaves to growing nonphotosynthetic organs such as roots and seeds. These growing tissues, besides carbohydrate supply, require uptake of water through aquaporins to enhance cell expansion during growth. Previous work revealed Sucrose Induced Receptor Kinase, SIRK1, to control aquaporin activity via phosphorylation in response to external sucrose stimulation. Here, we present the regulatory role of AT3G02880 (QSK1), a receptor kinase with a short external domain, in modulation of SIRK1 activity. Our results suggest that SIRK1 autophosphorylates at Ser-744 after sucrose treatment. Autophosphorylated SIRK1 then interacts with and transphosphorylates QSK1 and QSK2. Upon interaction with QSK1, SIRK1 phosphorylates aquaporins at their regulatory C-terminal phosphorylation sites. Consequently, in root protoplast swelling assays, the
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