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.

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.

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 A SNARE Complex Unique to Seed Plants Is Required for Protein Storage Vacuole Biogenesis and Seed Development of Arabidopsis thaliana

2008 ◽  
Vol 20 (11) ◽  
pp. 3006-3021 ◽  
Author(s):  
Kazuo Ebine ◽  
Yusuke Okatani ◽  
Tomohiro Uemura ◽  
Tatsuaki Goh ◽  
Keiko Shoda ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Seed Development ◽  
Snare Complex ◽  
Seed Plants ◽  
Protein Storage ◽  
Protein Storage Vacuole ◽  
Vacuole Biogenesis ◽  
Storage Vacuole

scholarly journals Protein storage vacuoles form de novo during pea cotyledon development

1995 ◽  
Vol 108 (1) ◽  
pp. 299-310 ◽  
Author(s):  
B. Hoh ◽  
G. Hinz ◽  
B.K. Jeong ◽  
D.G. Robinson
Keyword(s):  
Membrane Protein ◽  
De Novo ◽  
Storage Proteins ◽  
Protein Body ◽  
Membrane System ◽  
Intermediate Stage ◽  
Integral Membrane Protein ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Protein Storage Vacuole

We have investigated the formation of protein storage vacuoles in peas (Pisum sativum L.) in order to determine whether this organelle arises de novo during cotyledon development. A comparison of different stages in cotyledon development indicates that soluble protease activities decline and the amounts of storage proteins and the integral membrane protein of the protein body, alpha-TIP, increase during seed maturation. On linear sucrose density gradients we have been able to distinguish between two separate vesicle populations: one enriched in alpha-TIP, and one in TIP-Ma 27, a membrane protein characteristic of vegetative vacuoles. Both vesicle populations possess, however, PPase and V-ATPase activities. Conventionally fixed cotyledonary tissue at an intermediate stage in cotyledon development reveals the presence of a complex tubular-cisternal membrane system that seems to surround the pre-existing vacuoles. The latter gradually become compressed as a result of dilation of the former membrane system. This was confirmed immunocytochemically with the TIP-Ma 27 antiserum. Deposits of the storage proteins vicilin and legumin in the lumen, and the presence of alpha-TIP in the membranes of the expanding membrane system provide evidence of its identity as a precursor to the protein storage vacuole.

α-Galactosidase is synthesized in tomato seeds during development and is localized in the protein storage vacuoles

2001 ◽  
Vol 79 (12) ◽  
pp. 1417-1424 ◽  
Author(s):  
George W Bassel ◽  
Robert T Mullen ◽  
J Derek Bewley
Keyword(s):  
Subcellular Fractionation ◽  
Chloramphenicol Acetyltransferase ◽  
Tonoplast Intrinsic Protein ◽  
Intracellular Location ◽  
Protein Storage ◽  
Intrinsic Protein ◽  
Protein Storage Vacuoles ◽  
Tomato Seeds ◽  
Protein Storage Vacuole ◽  
Storage Vacuole

The localization of the enzyme α-galactosidase (EC 3.2.1.22) was investigated during its synthesis in developing tomato (Lycopersicon esculentum Mill.) cv. Trust seeds. This enzyme is also present in germinating seeds, where it is involved in the mobilization of carbohydrate reserves during and following seed germination. Subcellular fractionation of developing tomato seeds revealed that there is a cosedimentation between α-galactosidase activity and protein storage vacuoles in a density gradient, which is dependent upon the presence of membranes. A second approach to localizing this enzyme involved the transient transformation of protoplasts from developing tomato seeds. A reporter construct, coding for tomato α-galactosidase, fused N-terminally to the bacterial enzyme chloramphenicol acetyltransferase was used for transient expression. Immunofluorescence microscopy revealed a colocalization between the α-galactosidase - chloramphenicol acetyltransferase fusion protein and the α-tonoplast intrinsic protein, and a partial colocalization with the dark intrinsic protein (both vacuolar proteins). These data indicate that the protein storage vacuole is the intracellular location for α-galactosidase in developing tomato seeds.Key words: α-galactosidase, protein storage vacuole, seed development, seed protoplasts, tomato, tonoplast intrinsic protein.

scholarly journals Biogenesis of the Protein Storage Vacuole Crystalloid

2000 ◽  
Vol 150 (4) ◽  
pp. 755-770 ◽  
Author(s):  
Liwen Jiang ◽  
Thomas E. Phillips ◽  
Sally W. Rogers ◽  
John C. Rogers
Keyword(s):  
Seed Protein ◽  
Animal Cells ◽  
Reporter Protein ◽  
Developmentally Regulated ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Protein Storage Vacuole ◽  
Vacuolar System ◽  
Unique Mechanism ◽  
Storage Vacuole

We identify new organelles associated with the vacuolar system in plant cells. These organelles are defined biochemically by their internal content of three integral membrane proteins: a chimeric reporter protein that moves there directly from the ER; a specific tonoplast intrinsic protein; and a novel receptor-like RING-H2 protein that traffics through the Golgi apparatus. Highly conserved homologues of the latter are expressed in animal cells. In a developmentally regulated manner, the organelles are taken up into vacuoles where, in seed protein storage vacuoles, they form a membrane-containing crystalloid. The uptake and preservation of the contents of these organelles in vacuoles represents a unique mechanism for compartmentalization of protein and lipid for storage.

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