Fusion, rupture, and degeneration: the fate of in vivo-labelled PSVs in developing barley endosperm*

Ibl, Verena; Kapusi, Eszter; Arcalís, Elsa; Kawagoe, Yasuhiro; Stöger, Eva

doi:10.1093/jxb/eru175

Cited by 22 publications

(50 citation statements)

References 46 publications

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“…Additionally, the seed weight between the stages are significantly different except the stage between 6 and 10 DAP ( Supplementary Fig. S2e) These results are in line with the previously published microscopic data where the most dramatic endomembrane rearrangements could be observed between 8 and 12 DAP 13 .…”

Section: Multivariate Statistics Unravel Proteome Reorganization Acrosupporting

confidence: 91%

“…3a-c). PBs are identified in the bright field as small spherical structures as recently published 13,15,16 . Interestingly, a faint actin signal was observed at the plasma membrane at ≥20 DAP, whereas the signal of tubulin at the plasma membrane was strong at 6 DAP but was reduced at 12 and ≥20 DAP ( Fig.…”

Section: Development Phase I Contains Proteins Of High Abundance Assomentioning

confidence: 85%

“…Live cell imaging. GP and the transgenic line TIP3-GFP 13 were used for live cell imaging as previously described 13 . ER-Tracker Green (BODIPY FL Glibenclamide; #E34251, Thermo Fisher Scientific, Waltham, Massachusetts, USA) and LysoTracker Red DND-99 (#L7528, Thermo Fisher Scientific, Waltham, Massachusetts, USA) were used to visualize ER and acidic compartments, respectively.…”

Section: Microscopymentioning

confidence: 99%

“…ER-Tracker Green (BODIPY FL Glibenclamide; #E34251, Thermo Fisher Scientific, Waltham, Massachusetts, USA) and LysoTracker Red DND-99 (#L7528, Thermo Fisher Scientific, Waltham, Massachusetts, USA) were used to visualize ER and acidic compartments, respectively. ER-Tracker Green was used as previously described 13 . In detail, at least three randomly selected transgenic and GP grains were harvested at 6, 12 and ≥20 DAP, sectioned, washed, and stained as follows: ER-Tracker Green, 1 h (final concentration, 2 µM, from 1 mM DMSO stock with water); LysoTracker Red, 30 min (final concentration, 2 µM, from 1 mM DMSO stock with water).…”

Section: Microscopymentioning

confidence: 99%

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Protein sorting into protein bodies during barley endosperm development is putatively regulated by cytoskeleton members, MVBs and the HvSNF7s

Roustan

Hilscher

Weidinger

et al. 2020

Sci Rep

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cereal endosperm is a short-lived tissue adapted for nutrient storage, containing specialized organelles, such as protein bodies (pBs) and protein storage vacuoles (pSVs), for the accumulation of storage proteins. During development, protein trafficking and storage require an extensive reorganization of the endomembrane system. Consequently, endomembrane-modifying proteins will influence the final grain quality and yield. However, little is known about the molecular mechanism underlying endomembrane system remodeling during barley grain development. By using label-free quantitative proteomics profiling, we quantified 1,822 proteins across developing barley grains. Based on proteome annotation and a homology search, 94 proteins associated with the endomembrane system were identified that exhibited significant changes in abundance during grain development. Clustering analysis allowed characterization of three different development phases; notably, integration of proteomics data with in situ subcellular microscopic analyses showed a high abundance of cytoskeleton proteins associated with acidified PBs at the early development stages. Moreover, endosomal sorting complex required for transport (ESCRT)-related proteins and their transcripts are most abundant at early and mid-development. Specifically, multivesicular bodies (MVBs), and the ESCRT-III HvSNF7 proteins are associated with PBs during barley endosperm development. Together our data identified promising targets to be genetically engineered to modulate seed storage protein accumulation that have a growing role in health and nutritional issues. After differentiation, fully developed cereal endosperm makes up to 75% of the grain weight and covers four major cell types: aleurone, starchy endosperm, transfer cells, and the cells of the embryo surrounding region 1. The starchy endosperm thereby is characterized as a storage site, accumulating starch and seed storage proteins (SSPs) 2. The aleurone layer plays essential roles during seed germination and mobilizes starch and SSP reserves in the starchy endosperm by releasing hydrolytic enzymes that are responsible for the degradation of stored nutrients in the endosperm 2. Contrary to the persistent endosperm of cereals, the cellular endosperm of Arabidopsis thaliana (A. thaliana) supports the developing and growing embryo, resulting in a gradually depleted endosperm as the embryo grows. Finally, the massive A. thaliana embryo is only accompanied by a single peripheral layer, the aleurone layer, in mature seeds 2. Consequently, A. thaliana cannot to be used as a model system to study the endomembrane system in grain endosperm.

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Section: Multivariate Statistics Unravel Proteome Reorganization Acrosupporting

confidence: 91%

Section: Development Phase I Contains Proteins Of High Abundance Assomentioning

confidence: 85%

Section: Microscopymentioning

confidence: 99%

Section: Microscopymentioning

confidence: 99%

See 2 more Smart Citations

Protein sorting into protein bodies during barley endosperm development is putatively regulated by cytoskeleton members, MVBs and the HvSNF7s

Roustan

Hilscher

Weidinger

et al. 2020

Sci Rep

Self Cite

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“…Generated hydrogen peroxide might serve as a signal introducing the programmed cell death and subsequently kernel desiccation (Onda et al, 2009). More recently, Ibl et al (2014) suggested that both the membrane shrinkage and degeneration of PB occurred before PB development were completed in barley endosperm cells. The synthesis of vast amounts of disulfide-rich storage proteins during grain-filling (Figure 4E and G) might be accompanied by the production of hydrogen peroxide in ER, resulting in the peroxidation of membrane lipids under normal conditions (Sattler et al, 2006; Onda et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

Multiple strategies for heat adaptation in rice endosperms revealed by on-site cell-specific analysis

Wada

Hatakeyama

Onda

et al. 2017

Preprint

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19Plant cells have multiple strategies to adapt to environmental stresses. Rice endosperms 20 form chalkiness in a part of the tissue under heat conditions during the grain-filling stage, 21 although nitrogen supply reduces chalky rice. Air spaces formed in the cells cause an 22 irregular light reflection and create chalkiness, yet what exactly occurs remains unclear at 23 cell level. Through on-site cell-specific analysis, we show that heat-treated cells adjust 24 osmotically and retard protein synthesis to preserve protein storage vacuoles in the cytosol, 25 resulting in air space formation. Application of nitrogen enhances heat tolerance to sustain 26 protein body and amyloplast development during strong osmotic adjustment, which 27 diminishes air spaces to avoid chalkiness. Hence, we conclude that rice endosperm cells 28 could alter organelle compartments spatially during the heat adaptation, depending on the 29 available nitrogen level. Our findings provide new insight into the cellular mechanism of rice 30 chalky formation as a strategy for heat acclimation.

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Endomembrane‐mediated storage protein trafficking in plants: Golgi‐dependent or Golgi‐independent?

et al. 2022

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Seed storage proteins (SSPs) accumulated within plant seeds constitute the major protein nutrition sources for human and livestock. SSPs are synthesized on the endoplasmic reticulum and are then deposited in plant-specific protein bodies, including endoplasmic reticulum-derived protein bodies and protein storage vacuoles. Plant seeds have evolved a distinct endomembrane system to accomplish SSP transport. There are two distinct types of trafficking pathways contributing to SSP delivery to protein storage vacuoles: one is Golgi-dependent and the other is Golgi-independent. In recent years, molecular, genetic, and biochemical studies have shed light on the complex network controlling SSP trafficking, to which both evolutionarily conserved molecular machineries and plant-unique regulators contribute. In this review, we discuss current knowledge of protein body biogenesis and endomembrane-mediated SSP transport, focusing on endoplasmic reticulum export and post-Golgi traffic. This knowledge supports a dominant role for the Golgi-dependent pathways in SSP transport in Arabidopsis and rice. In addition, we describe cutting-edge strategies for dissecting the endomembrane trafficking system in plant seeds to advance the field.

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Fusion, rupture, and degeneration: the fate of in vivo-labelled PSVs in developing barley endosperm*

Abstract: SummaryThe article provides in vivo imaging data on the morphological changes in the endomembrane architecture of developing barley seeds, focussing on the fate of protein storage vacuoles along endosperm development.

Cited by 22 publications

References 46 publications

Protein sorting into protein bodies during barley endosperm development is putatively regulated by cytoskeleton members, MVBs and the HvSNF7s

Protein sorting into protein bodies during barley endosperm development is putatively regulated by cytoskeleton members, MVBs and the HvSNF7s

Multiple strategies for heat adaptation in rice endosperms revealed by on-site cell-specific analysis

Endomembrane‐mediated storage protein trafficking in plants: Golgi‐dependent or Golgi‐independent?

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