Evidence map›Paper›PMID 38506228›Full record

ArticleJournal of cell science2024

Role of the dynamin-related protein 2 family and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana.

Nataliia Gnyliukh, Alexander Johnson, Marie-Kristin Nagel, Aline Monzer, David Babić, Annamaria Hlavata, Saqer S Alotaibi, Erika Isono, Martin Loose, Jiří Friml

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. 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

10 authors at 4 institutions in 3 countries.

Nataliia GnyliukhInstitute of Science and Technology Austria (ISTA), 3400 Klosterneuburg, Austria.ORCID 0000-0002-2198-0509
Alexander JohnsonDivision of Anatomy, Centre for Anatomy & Cell Biology, Medical University of Vienna, 1090 Vienna, Austria.ORCID 0000-0002-2739-8843
Marie-Kristin NagelDepartment of Biology, University of Konstanz, 78464 Konstanz, Germany.
Aline MonzerInstitute of Science and Technology Austria (ISTA), 3400 Klosterneuburg, Austria.
David BabićInstitute of Science and Technology Austria (ISTA), 3400 Klosterneuburg, Austria.
Annamaria HlavataInstitute of Science and Technology Austria (ISTA), 3400 Klosterneuburg, Austria.
Saqer S AlotaibiDepartment of Biotechnology, College of Science, Taif University, Taif 21944, Saudi Arabia.
Erika IsonoDepartment of Biology, University of Konstanz, 78464 Konstanz, Germany.
Martin LooseInstitute of Science and Technology Austria (ISTA), 3400 Klosterneuburg, Austria.
Jiří FrimlInstitute of Science and Technology Austria (ISTA), 3400 Klosterneuburg, Austria.ORCID 0000-0002-8302-7596
Institute of Science and Technology Austria · ATUniversity of Konstanz · DEMedical University of Vienna · ATTaif University · SA

Funding

Austrian Science Fund I 6123-BEuropean Union's Horizon 2020 research and innovation program (2018-2020) under the Marie Sklodowska-Curie Grant 665385Horizon 2020 665385Institute of Science and Technology AustriaTaif University TURSP-HC2022/02Taif University Researchers Supporting Project TURSP-HC2022/02
6 · The paper itself

Abstract

Clathrin-mediated endocytosis (CME) is vital for the regulation of plant growth and development through controlling plasma membrane protein composition and cargo uptake. CME relies on the precise recruitment of regulators for vesicle maturation and release. Homologues of components of mammalian vesicle scission are strong candidates to be part of the scission machinery in plants, but the precise roles of these proteins in this process are not fully understood. Here, we characterised the roles of the plant dynamin-related protein 2 (DRP2) family (hereafter DRP2s) and SH3-domain containing protein 2 (SH3P2), the plant homologue to recruiters of dynamins, such as endophilin and amphiphysin, in CME by combining high-resolution imaging of endocytic events in vivo and characterisation of the purified proteins in vitro. Although DRP2s and SH3P2 arrive similarly late during CME and physically interact, genetic analysis of the sh3p123 triple mutant and complementation assays with non-SH3P2-interacting DRP2 variants suggest that SH3P2 does not directly recruit DRP2s to the site of endocytosis. These observations imply that, despite the presence of many well-conserved endocytic components, plants have acquired a distinct mechanism for CME.

Indexed as

ArabidopsisArabidopsis ProteinsDynaminsEndocytosisCarrier ProteinsClathrinGTP-Binding ProteinsMutationArabidopsis ProteinsCarrier ProteinsClathrinDynaminsGTP-Binding ProteinsSH3P2 protein, ArabidopsisArabidopsis thalianaClathrin-mediated endocytosisDynamin-related protein 2SH3P2Total internal reflection fluorescence microscopyVesicle scission

Identifiers

PMID38506228
PMCPMC11112126
OpenAlexW4393026556

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.