Evidence map›Paper›PMID 34907016›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

The TPLATE complex mediates membrane bending during plant clathrin-mediated endocytosis.

Alexander Johnson, Dana A Dahhan, Nataliia Gnyliukh, Walter A Kaufmann, Vanessa Zheden, Tommaso Costanzo, Pierre Mahou, Mónika Hrtyan, Jie Wang, Juan Aguilera-Servin and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 38 citations in OpenAlex.

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  4. Clathrin-mediated endocytosis of ERECTA family receptors is essential for proper stomatal development inProceedings of the National Academy of Sciences of the United States of America · 2026
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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

15 authors at 4 institutions in 4 countries.

Alexander JohnsonInstitute of Science and Technology, 3400 Klosterneuburg, Austria.ORCID 0000-0002-2739-8843
Dana A DahhanDepartment of Biochemistry, Hector F. DeLuca Laboratories, University of Wisconsin-Madison, Madison, WI 53706.ORCID 0000-0002-6079-4434
Nataliia GnyliukhInstitute of Science and Technology, 3400 Klosterneuburg, Austria.
Walter A KaufmannInstitute of Science and Technology, 3400 Klosterneuburg, Austria.
Vanessa ZhedenInstitute of Science and Technology, 3400 Klosterneuburg, Austria.ORCID 0000-0002-9438-4783
Tommaso CostanzoInstitute of Science and Technology, 3400 Klosterneuburg, Austria.ORCID 0000-0001-9732-3815
Pierre MahouCNRS, INSERM, Laboratory for Optics and Biosciences Ecole Polytechnique, Institut Polytechnique de Paris, 91128 Palaiseau, France.ORCID 0000-0003-4452-1011
Mónika HrtyanInstitute of Science and Technology, 3400 Klosterneuburg, Austria.
Jie WangDepartment of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.
Juan Aguilera-ServinInstitute of Science and Technology, 3400 Klosterneuburg, Austria.
Daniël van DammeDepartment of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium.
Emmanuel BeaurepaireCNRS, INSERM, Laboratory for Optics and Biosciences Ecole Polytechnique, Institut Polytechnique de Paris, 91128 Palaiseau, France.ORCID 0000-0002-2082-8214
Martin LooseInstitute of Science and Technology, 3400 Klosterneuburg, Austria.
Sebastian Y BednarekDepartment of Biochemistry, Hector F. DeLuca Laboratories, University of Wisconsin-Madison, Madison, WI 53706.
Jiří FrimlInstitute of Science and Technology, 3400 Klosterneuburg, Austria; jiri.friml@ist.ac.at.ORCID 0000-0002-8302-7596
Institute of Science and Technology Austria · ATCentre National de la Recherche Scientifique · FRGhent University · BEUniversity of Wisconsin–Madison · US

Funding

Austrian Science Fund FWF I 3630European Research Council 682436
6 · The paper itself

Abstract

Clathrin-mediated endocytosis is the major route of entry of cargos into cells and thus underpins many physiological processes. During endocytosis, an area of flat membrane is remodeled by proteins to create a spherical vesicle against intracellular forces. The protein machinery which mediates this membrane bending in plants is unknown. However, it is known that plant endocytosis is actin independent, thus indicating that plants utilize a unique mechanism to mediate membrane bending against high-turgor pressure compared to other model systems. Here, we investigate the TPLATE complex, a plant-specific endocytosis protein complex. It has been thought to function as a classical adaptor functioning underneath the clathrin coat. However, by using biochemical and advanced live microscopy approaches, we found that TPLATE is peripherally associated with clathrin-coated vesicles and localizes at the rim of endocytosis events. As this localization is more fitting to the protein machinery involved in membrane bending during endocytosis, we examined cells in which the TPLATE complex was disrupted and found that the clathrin structures present as flat patches. This suggests a requirement of the TPLATE complex for membrane bending during plant clathrin-mediated endocytosis. Next, we used in vitro biophysical assays to confirm that the TPLATE complex possesses protein domains with intrinsic membrane remodeling activity. These results redefine the role of the TPLATE complex and implicate it as a key component of the evolutionarily distinct plant endocytosis mechanism, which mediates endocytic membrane bending against the high-turgor pressure in plant cells.

Indexed as

ArabidopsisArabidopsis ProteinsCell MembraneClathrinEndocytosisFluorescent DyesMicroscopy, Electron, Scanning TransmissionMicroscopy, FluorescencePlant CellsSeedlingsArabidopsis ProteinsClathrinFluorescent DyesTPLATE protein, ArabidopsisArabidopsisclathrin-mediated endocytosismembrane remodelingTPLATE

Identifiers

PMID34907016
PMCPMC8691179
OpenAlexW4226148212

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.