ArticlePlant physiology2004
Phosphorylation of the amino terminus of maize sucrose synthase in relation to membrane association and enzyme activity.
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 35 papers.
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Who cites it
35 citing papers in PubMed, 111 citations in OpenAlex.
- The Plant Sucrose Synthase Gene Family: Multi-Level Regulatory Networks and Functional Diversification in Plants.Biomolecules · 2026Review
- Article
- Comprehensive analysis of SDH genes in Populus and functional characterization of SDH4 in xylem and cambium development.BMC plant biology · 2025Article
- Sucrose synthase dynamics and its potential role in heat stress tolerance in cereals.Frontiers in plant science · 2025Review
- Allele-Specific Hormone Dynamics in Highly Transgressive F2 Biomass Segregants in Sugarcane (Plants (Basel, Switzerland) · 2024Article
- Article
- High Daytime Temperature Responsive MicroRNA Profiles in Developing Grains of Rice Varieties with Contrasting Chalkiness.International journal of molecular sciences · 2023Article
- Identification of sucrose synthase fromFrontiers in microbiology · 2023Article
- Systems-level proteomics and metabolomics reveals the diel molecular landscape of diverse kale cultivars.Frontiers in plant science · 2023Article
- Identification of Genetic Variations and Candidate Genes Responsible for Stalk Sugar Content and Agronomic Traits in Fresh Corn via GWAS across Multiple Environments.International journal of molecular sciences · 2022Article
- Purification and Biochemical Characterization ofInternational journal of molecular sciences · 2021Article
- Subcellular Targeting of Plant Sucrose Transporters Is Affected by Their Oligomeric State.Plants (Basel, Switzerland) · 2020Article
- Exploring natural genetic variation in tomato sucrose synthases on the basis of increased kinetic properties.PloS one · 2018Article
- Serine phosphorylation of the cotton cytosolic pyruvate kinase GhPK6 decreases its stability and activity.FEBS open bio · 2017Article
- Comparative Phosphoproteomic Analysis under High-Nitrogen Fertilizer Reveals Central Phosphoproteins Promoting Wheat Grain Starch and Protein Synthesis.Frontiers in plant science · 2017Article
- Heat stress affects the cytoskeleton and the delivery of sucrose synthase in tobacco pollen tubes.Planta · 2016Article
- Identification and Characterization of the Sucrose Synthase 2 Gene (Sus2) in Durum Wheat.Frontiers in plant science · 2016Article
- A Role for Barley Calcium-Dependent Protein Kinase CPK2a in the Response to Drought.Frontiers in plant science · 2016Article
- The Crystal Structure of Nitrosomonas europaea Sucrose Synthase Reveals Critical Conformational Changes and Insights into Sucrose Metabolism in Prokaryotes.Journal of bacteriology · 2015Article
- Biochemical and molecular characterization of RcSUS1, a cytosolic sucrose synthase phosphorylated in vivo at serine 11 in developing castor oil seeds.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sucrose synthase (SUS) is phosphorylated on a major, amino-terminal site located at Ser-15 (S15) in the maize (Zea mays) SUS1 protein. Site- and phospho-specific antibodies against a phosphorylated S15 (pS15) peptide allowed direct analysis of S15 phosphorylation in relation to membrane association. Immunoblots of the maize leaf elongation zone, divided into 4-cm segments, demonstrated that the abundance of soluble (s-SUS) and membrane (m-SUS) SUS protein showed distinct positional profiles. The content of m-SUS was maximal in the 4- to 8-cm segment where it represented 9% of total SUS and occurred as a peripheral membrane protein. In contrast, s-SUS was highest in the 12- to 16-cm segment. Relative to s-SUS, m-SUS was hypophosphorylated at S15 in the basal 4 cm but hyperphosphorylated in apical segments. Differing capabilities of the anti-pS15 and anti-S15 peptide antibodies to immunoprecipitate SUS suggested that phosphorylation of S15, or exposure of unphosphorylated SUS to slightly acidic pH, altered the structure of the amino terminus. These structural changes were generally coincident with the increased sucrose cleavage activity that occurs at pH values below 7.5. In vitro S15 phosphorylation of the S170A SUS protein by a maize calcium-dependent protein kinase (CDPK) significantly increased sucrose cleavage activity at low pH. Collectively, the results suggest that (1) SUS membrane binding is controlled in vivo; (2) relative pS15 content of m-SUS depends on the developmental state of the organ; and (3) phosphorylation of S15 affects amino-terminal conformation in a way that may stimulate the catalytic activity of SUS and influence membrane association.
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