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Open AccessArticle

N-Linked Glycosylation Modulates Golgi-Independent Vacuolar Sorting Mediated by the Plant Specific Insert

1
Faculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, s/nº, 4169-007 Porto, Portugal
2
Instituto Gulbenkian de Ciência, Rua da Quinta Grande 6, 2780-156 Oeiras, Portugal
3
GreenUPorto-Sustainable Agrifood Production Research Center, Campus de Vairão, Rua Padre Armando Quintas 7, 4485-661 Vila do Conde, Portugal
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Plants 2019, 8(9), 312; https://doi.org/10.3390/plants8090312
Received: 31 July 2019 / Revised: 23 August 2019 / Accepted: 28 August 2019 / Published: 30 August 2019
(This article belongs to the Special Issue Plant Endomembranes Organization and Trafficking)
In plant cells, the conventional route to the vacuole involves the endoplasmic reticulum, the Golgi and the prevacuolar compartment. However, over the years, unconventional sorting to the vacuole, bypassing the Golgi, has been described, which is the case of the Plant-Specific Insert (PSI) of the aspartic proteinase cardosin A. Interestingly, this Golgi-bypass ability is not a characteristic shared by all PSIs, since two related PSIs showed to have different sensitivity to ER-to-Golgi blockage. Given the high sequence similarity between the PSI domains, we sought to depict the differences in terms of post-translational modifications. In fact, one feature that draws our attention is that one is N-glycosylated and the other one is not. Using site-directed mutagenesis to obtain mutated versions of the two PSIs, with and without the glycosylation motif, we observed that altering the glycosylation pattern interferes with the trafficking of the protein as the non-glycosylated PSI-B, unlike its native glycosylated form, is able to bypass ER-to-Golgi blockage and accumulate in the vacuole. This is also true when the PSI domain is analyzed in the context of the full-length cardosin. Regardless of opening exciting research gaps, the results obtained so far need a more comprehensive study of the mechanisms behind this unconventional direct sorting to the vacuole. View Full-Text
Keywords: Plant Specific Insert; Aspartic proteinase; vacuolar sorting; unconventional trafficking; endoplasmic reticulum; Golgi; N-linked glycosylation Plant Specific Insert; Aspartic proteinase; vacuolar sorting; unconventional trafficking; endoplasmic reticulum; Golgi; N-linked glycosylation
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Vieira, V.; Peixoto, B.; Costa, M.; Pereira, S.; Pissarra, J.; Pereira, C. N-Linked Glycosylation Modulates Golgi-Independent Vacuolar Sorting Mediated by the Plant Specific Insert. Plants 2019, 8, 312.

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