Evidence map›Paper›PMID 31480247›Full record

ArticlePlants (Basel, Switzerland)2019

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

Vanessa Vieira, Bruno Peixoto, Mónica Costa, Susana Pereira, José Pissarra, Cláudia Pereira

Open access · goldAbstract read
In one paragraph

Article in Plants (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.4field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Unconventional Pathways of Protein Secretion: MammalsFrontiers in cell and developmental biology · 2022
    Review
  7. Article
  8. PSI relieves the pressure of membrane fusion.The Journal of biological chemistry · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Vanessa VieiraFaculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, s/nº, 4169-007 Porto, Portugal.
Bruno PeixotoFaculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, s/nº, 4169-007 Porto, Portugal.ORCID 0000-0002-1022-3908
Mónica CostaFaculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, s/nº, 4169-007 Porto, Portugal.
Susana PereiraFaculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, s/nº, 4169-007 Porto, Portugal.
José PissarraFaculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, s/nº, 4169-007 Porto, Portugal.
Cláudia PereiraFaculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, s/nº, 4169-007 Porto, Portugal. cpereira@fc.up.pt.ORCID 0000-0001-8050-5102
Universidade do Porto · PT

Funding

Fundação para a Ciência e Tecnologia PTDC/BIA-FBT/32013/2017
6 · The paper itself

Abstract

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.

Indexed as

Aspartic proteinaseendoplasmic reticulumGolgiN-linked glycosylationPlant Specific Insertunconventional traffickingvacuolar sorting

Identifiers

PMID31480247
PMCPMC6784193
OpenAlexW2970341624

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.