Evidence map›Paper›PMID 29440677›Full record

ArticleNature communications2018

Nanobody-triggered lockdown of VSRs reveals ligand reloading in the Golgi.

Simone Früholz, Florian Fäßler, Üner Kolukisaoglu, Peter Pimpl

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Article
  2. Article
  3. Cargo Sorting Zones in Plant Trans-Golgi Network.Sub-cellular biochemistry · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. An unexpected function for an ESCRT protein.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Plant ESCRT protein ALIX coordinates with retromer complex in regulating receptor-mediated sorting of soluble vacuolar proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. 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 · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. On the discovery of an endomembrane compartment in plants.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. MTV proteins unveil ER- and microtubule-associated compartments in the plant vacuolar trafficking pathway.Proceedings of the National Academy of Sciences of the United States of America · 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

4 authors.

Simone FrüholzCenter for Plant Molecular Biology (ZMBP), University of Tübingen, Auf der Morgenstelle 32, 72076, Tübingen, Germany.
Florian FäßlerCenter for Plant Molecular Biology (ZMBP), University of Tübingen, Auf der Morgenstelle 32, 72076, Tübingen, Germany.ORCID http://orcid.org/0000-0001-7149-769X
Üner KolukisaogluCenter for Plant Molecular Biology (ZMBP), University of Tübingen, Auf der Morgenstelle 32, 72076, Tübingen, Germany.
Peter PimplCenter for Plant Molecular Biology (ZMBP), University of Tübingen, Auf der Morgenstelle 32, 72076, Tübingen, Germany. pimpl@sustc.edu.cn.ORCID http://orcid.org/0000-0001-5031-8672

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein degradation in lytic compartments is crucial for eukaryotic cells. At the heart of this process, vacuolar sorting receptors (VSRs) bind soluble hydrolases in the secretory pathway and release them into the vacuolar route. Sorting efficiency is suggested to result from receptor recycling. However, how and to where plant VSRs recycle remains controversial. Here we present a nanobody-epitope interaction-based protein labeling and tracking approach to dissect their anterograde and retrograde transport routes in vivo. We simultaneously employ two different nanobody-epitope pairs: one for the location-specific post-translational fluorescence labeling of receptors and the other pair to trigger their compartment-specific lockdown via an endocytosed dual-epitope linker protein. We demonstrate VSR recycling from the TGN/EE, thereby identifying the cis-Golgi as the recycling target and show that recycled VSRs reload ligands. This is evidence that bidirectional VSR-mediated sorting of vacuolar proteins exists and occurs between the Golgi and the TGN/EE.

Indexed as

ArabidopsisEndocytosisEndosomesGolgi ApparatusLigandsNicotianaPisum sativumPlant ProteinsProtein Transporttrans-Golgi NetworkVacuolesLigandsPlant Proteins

Identifiers

PMID29440677
PMCPMC5811495

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.