Evidence map›Paper›PMID 23771894›Full record

ArticleThe Plant cell2013

MTV1 and MTV4 encode plant-specific ENTH and ARF GAP proteins that mediate clathrin-dependent trafficking of vacuolar cargo from the trans-Golgi network.

Michael Sauer, M Otilia Delgadillo, Jan Zouhar, Gregory D Reynolds, Janice G Pennington, Liwen Jiang, Sarah J Liljegren, York-Dieter Stierhof, Geert De Jaeger, Marisa S Otegui and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Cargo Sorting Zones in Plant Trans-Golgi Network.Sub-cellular biochemistry · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. The sorting of cargo proteins in the plantFrontiers in plant science · 2022
    Review
  10. Review
  11. Article
  12. EPSIN1 and MTV1 define functionally overlapping but molecularly distinctProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. On the discovery of an endomembrane compartment in plants.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. 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
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. 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

12 authors at 7 institutions in 5 countries.

Michael SauerDepartamento Molecular de Plantas, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Cientificas, 28049 Madrid, Spain.
M Otilia Delgadillo
Jan Zouhar
Gregory D Reynolds
Janice G Pennington
Liwen Jiang
Sarah J Liljegren
York-Dieter Stierhof
Geert De Jaeger
Marisa S Otegui
Sebastian Y Bednarek
Enrique Rojo
University of Wisconsin–Madison · USConsejo Superior de Investigaciones Científicas · ESCentro Nacional de Biotecnología · ESChinese University of Hong Kong · CNGhent University · BEUniversity of Mississippi · USUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many soluble proteins transit through the trans-Golgi network (TGN) and the prevacuolar compartment (PVC) en route to the vacuole, but our mechanistic understanding of this vectorial trafficking step in plants is limited. In particular, it is unknown whether clathrin-coated vesicles (CCVs) participate in this transport step. Through a screen for modified transport to the vacuole (mtv) mutants that secrete the vacuolar protein VAC2, we identified MTV1, which encodes an epsin N-terminal homology protein, and MTV4, which encodes the ADP ribosylation factor GTPase-activating protein nevershed/AGD5. MTV1 and NEV/AGD5 have overlapping expression patterns and interact genetically to transport vacuolar cargo and promote plant growth, but they have no apparent roles in protein secretion or endocytosis. MTV1 and NEV/AGD5 colocalize with clathrin at the TGN and are incorporated into CCVs. Importantly, mtv1 nev/agd5 double mutants show altered subcellular distribution of CCV cargo exported from the TGN. Moreover, MTV1 binds clathrin in vitro, and NEV/AGD5 associates in vivo with clathrin, directly linking these proteins to CCV formation. These results indicate that MTV1 and NEV/AGD5 are key effectors for CCV-mediated trafficking of vacuolar proteins from the TGN to the PVC in plants.

Indexed as

Amino Acid SequenceArabidopsis ProteinsClathrinGreen Fluorescent ProteinsGTPase-Activating ProteinsImmunoblottingMeristemMicroscopy, ConfocalMicroscopy, ElectronMolecular Sequence DataMutationPhylogenyPlants, Genetically ModifiedProtein BindingProtein TransportSequence Homology, Amino AcidArabidopsis ProteinsClathrinGreen Fluorescent ProteinsGTPase-Activating ProteinsMTV1 protein, ArabidopsisNEV protein, Arabidopsis

Identifiers

PMID23771894
PMCPMC3723622
OpenAlexW2168343784

What OpenQuestion holds

Textmetadata
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.