ArticleThe Plant cell2005
The critical role of disulfide bond formation in protein sorting in the endosperm of rice.
Article in The Plant cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 89 citations in OpenAlex.
- Structural characterization of OsPDIL2-3, a rice protein disulfide isomerase involved in prolamin accumulation.The Biochemical journal · 2026Article
- Multiplex CRISPR/Cas9 Editing of Rice Prolamin and GluA Glutelin Genes Reveals Subfamily-Specific Effects on Seed Protein Composition.Plants (Basel, Switzerland) · 2025Article
- OsSPL14 and OsNF-YB9/YC8-12 subunits cooperate to enhance grain appearance quality by promoting Waxy and PDIL1-1 expression in rice.Plant communications · 2025Article
- The challenges of co-extraction of animal and plant proteins from transgenic plants for use in food and feed.Frontiers in plant science · 2025Review
- Specialized endoplasmic reticulum-derived vesicles in plants: Functional diversity, evolution, and biotechnological exploitation.Journal of integrative plant biology · 2022Review
- Breeding Canola (Plants (Basel, Switzerland) · 2021Review
- Towards coeliac-safe bread.Plant biotechnology journal · 2020Article
- Glutelin subtype-dependent protein localization in rice grain evidenced by immunodetection analyses.Plant molecular biology · 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
- A conserved motif is essential for the correct assembly of proglutelins and for their export from the endoplasmic reticulum in rice endosperm.Journal of experimental botany · 2018Article
- Microscopic and Proteomic Analysis of Dissected Developing Barley Endosperm Layers Reveals the Starchy Endosperm as Prominent Storage Tissue for ER-Derived Hordeins Alongside the Accumulation of Barley Protein Disulfide Isomerase (HvPDIL1-1).Frontiers in plant science · 2018Article
- Accumulation of foreign polypeptides to rice seed protein body type I using prolamin portion sequences.Plant cell reports · 2017Article
- Where do Protein Bodies of Cereal Seeds Come From?Frontiers in plant science · 2016Review
- Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum.Frontiers in plant science · 2016Article
- Cellular disulfide bond formation in bioactive peptides and proteins.International journal of molecular sciences · 2015Review
- Protein accumulation in aleurone cells, sub-aleurone cells and the center starch endosperm of cereals.Plant cell reports · 2014Review
- Generation mechanism of novel, huge protein bodies containing wild type or hypoallergenic derivatives of birch pollen allergen Bet v 1 in rice endosperm.Plant molecular biology · 2014Article
- Protein body formation in the endoplasmic reticulum as an evolution of storage protein sorting to vacuoles: insights from maize γ-zein.Frontiers in plant science · 2014Article
- Effects of reduced prolamin on seed storage protein composition and the nutritional quality of rice.International journal of molecular sciences · 2013Article
- The oxidative protein folding machinery in plant cells.Protoplasma · 2013Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many seed storage proteins, including monomeric 2S albumin and polymeric prolamin, contain conserved sequences in three separate regions, termed A, B, and C, which contain the consensus motifs LxxC, CCxQL, and PxxC, respectively. Protein-sorting mechanisms in rice (Oryza sativa) endosperm were studied with a green fluorescent protein (GFP) fused to different segments of rice alpha-globulin, a monomeric, ABC-containing storage protein. The whole ABC region together with GFP was efficiently transported to protein storage vacuoles (type II protein bodies [PB-II]) in the endosperm cells and sequestered in the matrix that surrounds the crystalloids. Peptide Gln-23 to Ser-43 in the A region was sufficient to guide GFP to PB-II. However, GFP fused with the AB or B region accumulated in prolamin protein bodies. Substitution mutations in the CCxQL motif in the B region significantly altered protein localization in the endosperm cells. Furthermore, protein extracts containing these substituted proteins had increased amounts of the endoplasmic reticulum (ER) chaperons BiP (for binding protein), protein disulfide isomerase, and calnexin as a part of protein complexes that were insoluble in a detergent buffer. These results suggest that the ER chaperons and disulfide bonds formed at the dicysteine residues in CCxQL play critical roles in sorting fused proteins in the endosperm cells.
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