ArticleThe Journal of biological chemistry2014
Identification of multiple phosphorylation sites on maize endosperm starch branching enzyme IIb, a key enzyme in amylopectin biosynthesis.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 54 citations in OpenAlex.
- Discovering of the transcriptional regulatory network involved in starch biosynthesis in sorghum grains.Plant diversity · 2026Article
- Starch branching enzyme: structure, key functional sites, and regulation of starch characteristics and rice qualities.Plant cell reports · 2025Review
- Genome-Wide Dissection of Sorghum B3 Transcription Factor Family Identifies SbLAV1 as a Critical Transcriptional Regulator of Starch Biosynthesis in Developing Sorghum Grains.Plants (Basel, Switzerland) · 2025Article
- Dynamic Change in Starch Biosynthetic Enzymes Complexes during Grain-Filling Stages in BEIIb Active and Deficient Rice.International journal of molecular sciences · 2022Article
- Resistant starch formation in rice: Genetic regulation and beyond.Plant communications · 2022Review
- Starch Biosynthetic Protein Complex Formation in RiceJournal of applied glycoscience · 2022Article
- Starch branching enzymes as putative determinants of postharvest quality in horticultural crops.BMC plant biology · 2021Review
- Comparative Phosphoproteomic Analysis Reveals the Response of Starch Metabolism to High-Temperature Stress in Rice Endosperm.International journal of molecular sciences · 2021Article
- Starch biosynthesis in cereal endosperms: An updated review over the last decade.Plant communications · 2021Review
- A review of starch biosynthesis in cereal crops and its potential breeding applications in rice (PeerJ · 2021Article
- Inactivation of rice starch branching enzyme IIb triggers broad and unexpected changes in metabolism by transcriptional reprogramming.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Proteomic Analysis of Maize Endosperm Protein Enriched by Phos-tagInternational journal of molecular sciences · 2019Article
- Crop resistant starch and genetic improvement: a review of recent advances.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2018Review
- Rice Mutants Lacking Starch Synthase I or Branching Enzyme IIb Activity Altered Starch Biosynthetic Protein Complexes.Frontiers in plant science · 2018Article
- Bioinformatic andFrontiers in plant science · 2018Article
- Protein Kinases and Phosphatases of the Plastid and Their Potential Role in Starch Metabolism.Frontiers in plant science · 2018Review
- Article
- Internalization of the Extracellular Full-Length Tau Inside Neuro2A and Cortical Cells Is Enhanced by Phosphorylation.Biomolecules · 2016Article
- Formation of starch in plant cells.Cellular and molecular life sciences : CMLS · 2016Review
- Review
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Starch branching enzyme IIb (SBEIIb) plays a crucial role in amylopectin biosynthesis in maize endosperm by defining the structural and functional properties of storage starch and is regulated by protein phosphorylation. Native and recombinant maize SBEIIb were used as substrates for amyloplast protein kinases to identify phosphorylation sites on the protein. A multidisciplinary approach involving bioinformatics, site-directed mutagenesis, and mass spectrometry identified three phosphorylation sites at Ser residues: Ser(649), Ser(286), and Ser(297). Two Ca(2+)-dependent protein kinase activities were partially purified from amyloplasts, termed K1, responsible for Ser(649) and Ser(286) phosphorylation, and K2, responsible for Ser(649) and Ser(297) phosphorylation. The Ser(286) and Ser(297) phosphorylation sites are conserved in all plant branching enzymes and are located at opposite openings of the 8-stranded parallel β-barrel of the active site, which is involved with substrate binding and catalysis. Molecular dynamics simulation analysis indicates that phospho-Ser(297) forms a stable salt bridge with Arg(665), part of a conserved Cys-containing domain in plant branching enzymes. Ser(649) conservation appears confined to the enzyme in cereals and is not universal, and is presumably associated with functions specific to seed storage. The implications of SBEIIb phosphorylation are considered in terms of the role of the enzyme and the importance of starch biosynthesis for yield and biotechnological application.
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