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

• Type: Article in International Scientific Journal
• Date: 2019-08-30

Authors

Pereira, S (Author) FCUP; Vanessa Vieira (Author) Other; Bruno Peixoto (Author) Other; Mónica Costa (Author) Other; Pissarra, J (Author) FCUP; Claudia Pereira (Author) FCUP

Journal

Title: Plants

Vol. 8 No. 9

Pages: 312-312

Publisher: MDPI

Indexing

ISI Web of Knowledge - 6 Citations

Scopus - 7 Citations

DOAJ

Pubmed / Medline

Current Contents

Scientific classification

CORDIS: Natural sciences > Biological sciences > Biology > Molecular biology ; Natural sciences > Biological sciences > Botany > Plant physiology ; Natural sciences > Biological sciences > Botany > Phytopathology

FOS: Natural sciences > Biological sciences

Associated Projects

PTDC/BIA-FBT/32013/2017 - Remodelação de membranas sob stress: caracterização de determinantes proteicos e redes de interacção

Other information

Authenticus ID: P-00R-20P

DOI: 10.3390/plants8090312

Abstract (EN): 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 21