Evidence map›Paper›PMID 22635117›Full record

ArticlePlant physiology2012

An A/ENTH domain-containing protein functions as an adaptor for clathrin-coated vesicles on the growing cell plate in Arabidopsis root cells.

Kyungyoung Song, Mihue Jang, Soo Youn Kim, Goeun Lee, Gil-Je Lee, Dae Heon Kim, Yongjik Lee, Wonhwa Cho, Inhwan Hwang

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  9. Global Identification ofFrontiers in plant science · 2021
    Article
  10. Longin R-SNARE is retrieved from the plasma membrane by ANTH domain-containing proteins inProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Review
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  14. Regulation ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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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

9 authors at 2 institutions in 2 countries.

Kyungyoung SongDivision of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea.
Mihue Jang
Soo Youn Kim
Goeun Lee
Gil-Je Lee
Dae Heon Kim
Yongjik Lee
Wonhwa Cho
Inhwan Hwang
University of Illinois Chicago · USPohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytokinesis is the process of partitioning the cytoplasm of a dividing cell, thereby completing mitosis. Cytokinesis in the plant cell is achieved by the formation of a new cell wall between daughter nuclei using components carried in Golgi-derived vesicles that accumulate at the midplane of the phragmoplast and fuse to form the cell plate. Proteins that play major roles in the development of the cell plate in plant cells are not well defined. Here, we report that an AP180 amino-terminal homology/epsin amino-terminal homology domain-containing protein from Arabidopsis (Arabidopsis thaliana) is involved in clathrin-coated vesicle formation from the cell plate. Arabidopsis Epsin-like Clathrin Adaptor1 (AtECA1; At2g01600) and its homologous proteins AtECA2 and AtECA4 localize to the growing cell plate in cells undergoing cytokinesis and also to the plasma membrane and endosomes in nondividing cells. AtECA1 (At2g01600) does not localize to nascent cell plates but localizes at higher levels to expanding cell plates even after the cell plate fuses with the parental plasma membrane. The temporal and spatial localization patterns of AtECA1 overlap most closely with those of the clathrin light chain. In vitro protein interaction assays revealed that AtECA1 binds to the clathrin H chain via its carboxyl-terminal domain. These results suggest that these AP180 amino-terminal homology/epsin amino-terminal homology domain-containing proteins, AtECA1, AtECA2, and AtECA4, may function as adaptors of clathrin-coated vesicles budding from the cell plate.

Indexed as

CytokinesisAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportArabidopsisArabidopsis ProteinsCell MembraneClathrinClathrin-Coated VesiclesEndosomesGreen Fluorescent ProteinsPlant RootsProtein BindingProtein Structure, TertiaryProtein TransportProtoplastsRecombinant Fusion ProteinsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportArabidopsis ProteinsClathrinECA1 protein, ArabidopsisGreen Fluorescent ProteinsRecombinant Fusion Proteins

Identifiers

PMID22635117
PMCPMC3387690
OpenAlexW2030436482

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.