ArticleFrontiers in plant science2016
Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum.
Article in Frontiers in plant science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Recombinant production of spider silk protein in Physcomitrella photobioreactors.Plant cell reports · 2025Article
- Subcutaneous, Oral, and Intranasal Immunization of BALB/c Mice withTropical medicine and infectious disease · 2023Article
- 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
- 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
- Improving Protein Quantity and Quality-The Next Level of Plant Molecular Farming.International journal of molecular sciences · 2022Review
- Elastin-like polypeptide and γ-zein fusions significantly increase recombinant protein accumulation in soybean seeds.Transgenic research · 2021Article
- Recognition motifs rather than phylogenetic origin influence the ability of targeting peptides to import nuclear-encoded recombinant proteins into rice mitochondria.Transgenic research · 2020Article
- 3D Electron Microscopy Gives a Clue: Maize Zein Bodies Bud From Central Areas of ER Sheets.Frontiers in plant science · 2020Article
- Efficient Plant Production of Recombinant NS1 Protein for Diagnosis of Dengue.Frontiers in plant science · 2020Article
- Transient Expression of Dengue Virus NS1 Antigen inFrontiers in plant science · 2019Article
- Russell-Like Bodies in Plant Seeds Share Common Features With Prolamin Bodies and Occur Upon Recombinant Protein Production.Frontiers in plant science · 2019Article
- Dynamics of liquid-liquid phase separation of wheat gliadins.Scientific reports · 2018Article
- LALFPlant biotechnology journal · 2018Article
- Protein bodies: how the ER deals with high accumulation of recombinant proteins.Plant biotechnology journal · 2017Article
- Unlocking the full potential of plant cell-based production for valuable proteins: Challenges and innovative strategies.Biotechnology advancesReview
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein bodies (PBs) are organelles found in seeds whose main function is the storage of proteins that are used during germination for sustaining growth. PBs can also be induced to form in leaves when foreign proteins are produced at high levels in the endoplasmic reticulum (ER) and when fused to one of three tags: Zera®, elastin-like polypeptides (ELP), or hydrophobin-I (HFBI). In this study, we investigate the differences between ELP, HFBI and Zera PB formation, packing, and communication. Our results confirm the ER origin of all three fusion-tag-induced PBs. We show that secretory pathway proteins can be sequestered into all types of PBs but with different patterns, and that different fusion tags can target a specific protein to different PBs. Zera PBs are mobile and dependent on actomyosin motility similar to ELP and HFBI PBs. We show in vivo trafficking of proteins between PBs using GFP photoconversion. We also show that protein trafficking between ELP or HFBI PBs is faster and proteins travel further when compared to Zera PBs. Our results indicate that fusion-tag-induced PBs do not represent terminally stored cytosolic organelles, but that they form in, and remain part of the ER, and dynamically communicate with each other via the ER. We hypothesize that the previously documented PB mobility along the actin cytoskeleton is associated with ER movement rather than independent streaming of detached organelles.
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