scholarly journals OsVPS9A Functions Cooperatively with OsRAB5A to Regulate Post-Golgi Dense Vesicle-Mediated Storage Protein Trafficking to the Protein Storage Vacuole in Rice Endosperm Cells

2013 ◽  
Vol 6 (6) ◽  
pp. 1918-1932 ◽  
Author(s):  
Feng Liu ◽  
Yulong Ren ◽  
Yihua Wang ◽  
Cheng Peng ◽  
Kunneng Zhou ◽  
...  
Keyword(s):  
Protein Trafficking ◽  
Storage Protein ◽  
Rice Endosperm ◽  
Protein Storage ◽  
Protein Storage Vacuole ◽  
Storage Vacuole

The Trafficking Machinery of Lytic and Protein Storage Vacuoles: How Much is Shared and How Much is Distinct?

2021 ◽  
Author(s):  
Xiuxiu Zhang ◽  
Hui Li ◽  
Hai Lu ◽  
Inhwan Hwang
Keyword(s):  
Protein Trafficking ◽  
Molecular Mechanisms ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Protein Storage Vacuole ◽  
Lytic Vacuoles ◽  
Lytic Vacuole ◽  
The Relationship ◽  
Storage Vacuole ◽  
Made In

Abstract Plant cells contain two types of vacuoles, the lytic vacuole and the protein storage vacuole. Lytic vacuoles (LVs) are present in vegetative cells, whereas protein storage vacuoles (PSVs) are found in seed cells. The physiological functions of the two vacuole types differ. Newly synthesized proteins must be transported to these vacuoles via protein trafficking through the endomembrane system for them to function. Recently, significant advances have been made in elucidating the molecular mechanisms of protein trafficking to these organelles. Despite these advances, the relationship between the trafficking mechanisms in LV and PSVs remains unclear. Some aspects of the trafficking mechanisms are common to both organelles, but certain aspects are specific to trafficking to either LV or PSVs. In this review, we summarize recent findings on the components involved in protein trafficking to both LV and PSVs and compare them to examine the extent of overlap in the trafficking mechanisms. In addition, we discuss the interconnection between the LV and PSVs in protein trafficking machinery and the implication in the identity of these organelles.

scholarly journals Abiotic Stress Triggers the Expression of Genes Involved in Protein Storage Vacuole and Exocyst-Mediated Routes

2021 ◽  
Vol 22 (19) ◽  
pp. 10644
Author(s):  
João Neves ◽  
Miguel Sampaio ◽  
Ana Séneca ◽  
Susana Pereira ◽  
José Pissarra ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Protein Trafficking ◽  
Molecular Mechanisms ◽  
Ultrastructural Changes ◽  
Organelle Biogenesis ◽  
Morphological Alterations ◽  
Protein Storage ◽  
Expression Of Genes ◽  
Protein Storage Vacuole ◽  
Storage Vacuole

Adverse conditions caused by abiotic stress modulate plant development and growth by altering morphological and cellular mechanisms. Plants’ responses/adaptations to stress often involve changes in the distribution and sorting of specific proteins and molecules. Still, little attention has been given to the molecular mechanisms controlling these rearrangements. We tested the hypothesis that plants respond to stress by remodelling their endomembranes and adapting their trafficking pathways. We focused on the molecular machinery behind organelle biogenesis and protein trafficking under abiotic stress conditions, evaluating their effects at the subcellular level, by looking at ultrastructural changes and measuring the expression levels of genes involved in well-known intracellular routes. The results point to a differential response of the endomembrane system, showing that the genes involved in the pathway to the Protein Storage Vacuole and the exocyst-mediated routes are upregulated. In contrast, the ones involved in the route to the Lytic Vacuole are downregulated. These changes are accompanied by morphological alterations of endomembrane compartments. The data obtained demonstrate that plants’ response to abiotic stress involves the differential expression of genes related to protein trafficking machinery, which can be connected to the activation/deactivation of specific intracellular sorting pathways and lead to alterations in the cell ultrastructure.

scholarly journals AtRMR1 functions as a cargo receptor for protein trafficking to the protein storage vacuole

2005 ◽  
Vol 170 (5) ◽  
pp. 757-767 ◽  
Author(s):  
Misoon Park ◽  
Daeseok Lee ◽  
Gil-Je Lee ◽  
Inhwan Hwang
Keyword(s):  
Golgi Complex ◽  
Protein Trafficking ◽  
Transmembrane Domain ◽  
Binding Assays ◽  
Protein Storage ◽  
Final Destination ◽  
Protein Storage Vacuole ◽  
A Minor ◽  
Storage Vacuole

Organellar proteins are sorted by cargo receptors on the way to their final destination. However, receptors for proteins that are destined for the protein storage vacuole (PSV) are largely unknown. In this study, we investigated the biological role that Arabidopsis thaliana receptor homology region transmembrane domain ring H2 motif protein (AtRMR) 1 plays in protein trafficking to the PSV. AtRMR1 mainly colocalized to the prevacuolar compartment of the PSV, but a minor portion also localized to the Golgi complex. The coexpression of AtRMR1 mutants that were localized to the Golgi complex strongly inhibited the trafficking of phaseolin to the PSV and caused accumulation of phaseolin in the Golgi complex or its secretion. Coimmunoprecipitation and in vitro binding assays revealed that the lumenal domain of AtRMR1 interacts with the COOH-terminal sorting signal of phaseolin at acidic pH. Furthermore, phaseolin colocalized with AtRMR1 on its way to the PSV. Based on these results, we propose that AtRMR1 functions as the sorting receptor of phaseolin for its trafficking to the PSV.

scholarly journals Delivery of Prolamins to the Protein Storage Vacuole in Maize Aleurone Cells

2011 ◽  
Vol 23 (2) ◽  
pp. 769-784 ◽  
Author(s):  
Francisca C. Reyes ◽  
Taijoon Chung ◽  
David Holding ◽  
Rudolf Jung ◽  
Richard Vierstra ◽  
...  
Keyword(s):  
Protein Storage ◽  
Aleurone Cells ◽  
Protein Storage Vacuole ◽  
Storage Vacuole
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