Trafficking to the seed protein storage vacuole

2018 ◽  
Vol 45 (9) ◽  
pp. 895
Author(s):  
Joanne R. Ashnest ◽  
Anthony R. Gendall
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Storage ◽  
Protein Storage Vacuole ◽  
2S Albumins ◽  
Vacuolar Sorting ◽  
Mechanistic Understanding ◽  
Lytic Vacuole ◽  
Storage Vacuole

The processing and subcellular trafficking of seed storage proteins is a critical area of physiological, agricultural and biotechnological research. Trafficking to the lytic vacuole has been extensively discussed in recent years, without substantial distinction from trafficking to the protein storage vacuole (PSV). However, despite some overlap between these pathways, there are several examples of unique processing and machinery in the PSV pathway. Moreover, substantial new data has recently come to light regarding the important players in this pathway, in particular, the intracellular NHX proteins and their role in regulating lumenal pH. In some cases, these new data are limited to genetic evidence, with little mechanistic understanding. As such, the implications of these data in the current paradigm of PSV trafficking is perhaps yet unclear. Although it has generally been assumed that the major classes of storage proteins are trafficked via the same pathway, there is mounting evidence that the 12S globulins and 2S albumins may be trafficked independently. Advances in identification of vacuolar targeting signals, as well as an improved mechanistic understanding of various vacuolar sorting receptors, may reveal the differences in these trafficking pathways.

scholarly journals Vacuolar Storage Proteins Are Sorted in the Cis-Cisternae of the Pea Cotyledon Golgi Apparatus

2001 ◽  
Vol 152 (1) ◽  
pp. 41-50 ◽  
Author(s):  
Stefan Hillmer ◽  
Ali Movafeghi ◽  
David G. Robinson ◽  
Giselbert Hinz
Keyword(s):  
Golgi Apparatus ◽  
Storage Proteins ◽  
Spatial Separation ◽  
Golgi Stack ◽  
Protein Storage ◽  
Protein Storage Vacuole ◽  
Vacuolar Sorting ◽  
Sorting Receptor ◽  
Storage Vacuole ◽  
Dense Vesicles

Developing pea cotyledons contain functionally different vacuoles, a protein storage vacuole and a lytic vacuole. Lumenal as well as membrane proteins of the protein storage vacuole exit the Golgi apparatus in dense vesicles rather than in clathrin-coated vesicles (CCVs). Although the sorting receptor for vacuolar hydrolases BP-80 is present in CCVs, it is not detectable in dense vesicles. To localize these different vacuolar sorting events in the Golgi, we have compared the distribution of vacuolar storage proteins and of α-TIP, a membrane protein of the protein storage vacuole, with the distribution of the vacuolar sorting receptor BP-80 across the Golgi stack. Analysis of immunogold labeling from cryosections and from high pressure frozen samples has revealed a steep gradient in the distribution of the storage proteins within the Golgi stack. Intense labeling for storage proteins was registered for the cis-cisternae, contrasting with very low labeling for these antigens in the trans-cisternae. The distribution of BP-80 was the reverse, showing a peak in the trans-Golgi network with very low labeling of the cis-cisternae. These results indicate a spatial separation of different vacuolar sorting events in the Golgi apparatus of developing pea cotyledons.

scholarly journals The protein storage vacuole

2001 ◽  
Vol 155 (6) ◽  
pp. 991-1002 ◽  
Author(s):  
Liwen Jiang ◽  
Thomas E. Phillips ◽  
Christopher A. Hamm ◽  
Yolanda M. Drozdowicz ◽  
Philip A. Rea ◽  
...  
Keyword(s):  
Seed Development ◽  
Secretory Pathway ◽  
Storage Proteins ◽  
Plant Seed ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Protein Storage Vacuole ◽  
Membrane Bound ◽  
Lytic Vacuole ◽  
Storage Vacuole

Storage proteins are deposited into protein storage vacuoles (PSVs) during plant seed development and maturation and stably accumulate to high levels; subsequently, during germination the storage proteins are rapidly degraded to provide nutrients for use by the embryo. Here, we show that a PSV has within it a membrane-bound compartment containing crystals of phytic acid and proteins that are characteristic of a lytic vacuole. This compound organization, a vacuole within a vacuole whereby storage functions are separated from lytic functions, has not been described previously for organelles within the secretory pathway of eukaryotic cells. The partitioning of storage and lytic functions within the same vacuole may reflect the need to keep the functions separate during seed development and maturation and yet provide a ready source of digestive enzymes to initiate degradative processes early in germination.

scholarly journals Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana

2003 ◽  
Vol 100 (26) ◽  
pp. 16095-16100 ◽  
Author(s):  
T. Shimada ◽  
K. Fuji ◽  
K. Tamura ◽  
M. Kondo ◽  
M. Nishimura ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Vacuolar Sorting Receptor ◽  
Vacuolar Sorting ◽  
Sorting Receptor

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 Protein reservoirs of seeds are composites of amyloid and amyloid-like structures

2021 ◽  
Author(s):  
Nabodita Sinha ◽  
Avinash Y. Gahane ◽  
Talat Zahra ◽  
Ashwani K. Thakur
Keyword(s):  
Congo Red ◽  
Storage Proteins ◽  
Molecular Level ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Bodies ◽  
Molecular Rotor ◽  
Protein Storage ◽  
Enhanced Sensitivity ◽  
Amyloid Structures

AbstractSeed storage proteins, well-known for their nutritional functions are sequestered in protein bodies. However, their biophysical properties at the molecular level remain elusive. Based on the structure and function of protein bodies found in other organisms, we hypothesize that the seed protein bodies might be present as amyloid structures. When visualized with a molecular rotor Thioflavin-T and a recently discovered Proteostat® probe with enhanced sensitivity, the seed sections showed amyloid-like signatures in the protein storage bodies of the aleurone cells of monocots and cotyledon cells of dicots. To make the study compliant for amyloid detection, gold-standard Congo red dye was used. Positive apple-green birefringence due to Congo red affinity in some of the areas of ThT and Proteostat® binding, suggests the presence of both amyloid-like and amyloid deposits in the protein storage bodies. Further, diminishing amyloid signature in germinating seeds implies the degradation of these amyloid structures and their utilization. This study will open new research avenues for a detailed molecular-level understanding of the formation and utilization of aggregated protein bodies as well as their evolutionary roles.

scholarly journals A Vacuolar Sorting Receptor PV72 on the Membrane of Vesicles that Accumulate Precursors of Seed Storage Proteins (PAC Vesicles)

2002 ◽  
Vol 43 (10) ◽  
pp. 1086-1095 ◽  
Author(s):  
Tomoo Shimada ◽  
Etsuko Watanabe ◽  
Kentaro Tamura ◽  
Yasuko Hayashi ◽  
Mikio Nishimura ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Vacuolar Sorting Receptor ◽  
Vacuolar Sorting ◽  
Sorting Receptor
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