ArticlePlant molecular biology2006
The C-terminal region of alpha' subunit of soybean beta-conglycinin contains two types of vacuolar sorting determinants.
Article in Plant molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Structural insights into how vacuolar sorting receptor recognizes the C-terminal sorting determinant of a vicilin-like seed storage protein.The FEBS journal · 2026Article
- Subcellular localization of C-term-oleosin fused to β-casein reveals unexpected cytoplasmic accumulation in vacuole-targeted arabidopsis seeds.Frontiers in plant science · 2026Article
- Spatial activity mapping of ß-mannanase on soybean seeds.Scientific reports · 2024Article
- Genetic mapping and functional genomics of soybean seed protein.Molecular breeding : new strategies in plant improvement · 2023Article
- Soybean genetic resources contributing to sustainable protein production.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2022Review
- Structural insights into how vacuolar sorting receptors recognize the sorting determinants of seed storage proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Multiple internal sorting determinants can contribute to the trafficking of cruciferin to protein storage vacuoles.Plant molecular biology · 2015Article
- Delivering of proteins to the plant vacuole--an update.International journal of molecular sciences · 2014Review
- Accumulation of β-conglycinin in soybean cotyledon through the formation of disulfide bonds between α'- and α-subunits.Plant physiology · 2012Article
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3 authors at 1 institution in 1 country.
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Abstract
In maturing seed cells, proteins that accumulate in the protein storage vacuoles (PSVs) are synthesized on the endoplasmic reticulum (ER) and transported by vesicles to the PSVs. Vacuolar sorting determinants (VSDs) which are usually amino acid sequences of short or moderate length direct the proteins to this pathway. VSDs identified so far are classified into two types: sequence specific VSDs (ssVSDs) and C-terminal VSDs (ctVSDs). We previously demonstrated that VSDs of alpha' and beta subunits of beta-conglycinin, one of major storage proteins of soybean (Glycine max), reside in the C-terminal ten amino acids. Here we show that both types of VSDs coexist within this region of the alpha' subunit. Although ctVSDs can function only at the very C-termini of proteins, the C-terminal ten amino acids of alpha' subunit directed green fluorescent protein (GFP) to the PSVs even when they were placed at the N-terminus of GFP, indicating that an ssVSD resides in the sequence. By mutation analysis, it was found that the core sequence of the ssVSD is Ser-Ile-Leu (fifth to seventh residues counted from the C-terminus) which is conserved in the alpha and beta subunits and some vicilin-like proteins. On the other hand, the sequence composed of the C-terminal three amino acids (AFY) directed GFP to the PSVs when it was placed at the C-terminus of GFP, though the function as a VSD was disrupted at the N-terminus of GFP, indicating that the AFY sequence is a ctVSD.
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