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

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

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 Preliminary X-ray analysis of the binding domain of the soybean vacuolar sorting receptor complexed with a sorting determinant of a seed storage protein

2015 ◽  
Vol 71 (2) ◽  
pp. 132-135 ◽  
Author(s):  
Nobuyuki Maruyama ◽  
Tomohiro Goshi ◽  
Shigeru Sugiyama ◽  
Mayumi Niiyama ◽  
Hiroaki Adachi ◽  
...  
Keyword(s):  
Storage Protein ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Binding Domain ◽  
X Ray Diffraction ◽  
X Ray ◽  
Protein Storage Vacuoles ◽  
Vacuolar Sorting Receptor ◽  
Vacuolar Sorting ◽  
Sorting Receptor

β-Conglycinin is a major seed storage protein in soybeans, which are an important source of protein. The major subunits (α, α′ and β) of β-conglycinin are sorted to protein-storage vacuoles in seed cells. Vacuolar sorting receptor (VSR) is an integral membrane protein that recognizes the sorting determinant of vacuolar proteins, including β-conglycinin, and regulates their sorting process. Vacuolar sorting determinants of the α′ and β subunits of β-conglycinin exist in their C-terminal peptides. Here, the preliminary X-ray diffraction analysis of the binding domain of soybean VSR crystallized with the peptide responsible for the sorting determinant in β-conglycinin is reported. X-ray diffraction data were collected to a resolution of 3.5 Å. The crystals belonged to space groupP3121, with unit-cell parametersa=b= 116.4,c= 86.1 Å.

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