ArticleFrontiers in plant science2014
Protein body formation in the endoplasmic reticulum as an evolution of storage protein sorting to vacuoles: insights from maize γ-zein.
Article in Frontiers in plant science, 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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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Dynamic Changes in Amino Acid Release Patterns of Different Plant Protein Sources During In Vitro Digestion and Their Nutritional Value Assessment.Animals : an open access journal from MDPI · 2025Article
- Protein Biosynthesis and Maturation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Intracellular trafficking and glycosylation of hydroxyproline-O-glycosylation module in tobacco BY-2 cells is dependent on medium composition and transcriptome analysis.Scientific reports · 2023Article
- Generation of multi-layered protein bodies inFrontiers in plant science · 2023Article
- Alkaloid binding to opium poppy major latex proteins triggers structural modification and functional aggregation.Nature communications · 2022Article
- Specialized endoplasmic reticulum-derived vesicles in plants: Functional diversity, evolution, and biotechnological exploitation.Journal of integrative plant biology · 2022Review
- Wheat α-gliadin and high-molecular-weight glutenin subunit accumulate in different storage compartments of transgenic soybean seed.Transgenic research · 2022Article
- StresSeed: The Unfolded Protein Response During Seed Development.Frontiers in plant science · 2022Review
- Progressive Aggregation of 16 kDa Gamma-Zein during Seed Maturation in TransgenicInternational journal of molecular sciences · 2021Article
- Two γ-zeins induce the unfolded protein response.Plant physiology · 2021Article
- Towards coeliac-safe bread.Plant biotechnology journal · 2020Article
- A Review of Plant Vacuoles: Formation, Located Proteins, and Functions.Plants (Basel, Switzerland) · 2019Review
- NAC-type transcription factors regulate accumulation of starch and protein in maize seeds.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Russell-Like Bodies in Plant Seeds Share Common Features With Prolamin Bodies and Occur Upon Recombinant Protein Production.Frontiers in plant science · 2019Article
- Maize 16-kD γ-zein forms very unusual disulfide-bonded polymers in the endoplasmic reticulum: implications for prolamin evolution.Journal of experimental botany · 2018Article
- Comprehensive proteomic analysis of developing protein bodies in maize (Zea mays) endosperm provides novel insights into its biogenesis.Journal of experimental botany · 2016Article
- A Fusion between Domains of the Human Bone Morphogenetic Protein-2 and Maize 27 kD γ-Zein Accumulates to High Levels in the Endoplasmic Reticulum without Forming Protein Bodies in Transgenic Tobacco.Frontiers in plant science · 2016Article
- Where do Protein Bodies of Cereal Seeds Come From?Frontiers in plant science · 2016Review
- New insights into how seeds are made.Frontiers in plant science · 2015Article
- The Induction of Recombinant Protein Bodies in Different Subcellular Compartments Reveals a Cryptic Plastid-Targeting Signal in the 27-kDa γ-Zein Sequence.Frontiers in bioengineering and biotechnology · 2014Article
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Authors and funding
6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The albumin and globulin seed storage proteins present in all plants accumulate in storage vacuoles. Prolamins, which are the major proteins in cereal seeds and are present only there, instead accumulate within the endoplasmic reticulum (ER) lumen as very large insoluble polymers termed protein bodies. Inter-chain disulfide bonds play a major role in polymerization and insolubility of many prolamins. The N-terminal domain of the maize prolamin 27 kD γ-zein is able to promote protein body formation when fused to other proteins and contains seven cysteine residues involved in inter-chain bonds. We show that progressive substitution of these amino acids with serine residues in full length γ-zein leads to similarly progressive increase in solubility and availability to traffic from the ER along the secretory pathway. Total substitution results in very efficient secretion, whereas the presence of a single cysteine is sufficient to promote partial sorting to the vacuole via a wortmannin-sensitive pathway, similar to the traffic pathway of vacuolar storage proteins. We propose that the mechanism leading to accumulation of prolamins in the ER is a further evolutionary step of the one responsible for accumulation in storage vacuoles.
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