Evidence map›Paper›PMID 34757852›Full record

ArticleMolecular biology of the cell2022

The RabGAPs EPI64A and EPI64B regulate the apical structure of epithelial cells

Matthew R Miller, David J McDermitt, Cecile Sauvanet, Andrew T Lombardo, Riasat Zaman, Anthony Bretscher

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.1field-weighted citation impact, top 57% 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

5 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. On the mechanism of ezrin activation.Biophysical journal · 2026
    Article
  3. Article
  4. On the Mechanism of Ezrin Activation.bioRxiv : the preprint server for biology · 2025
    Article
  5. 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

6 authors at 1 institution in 1 country.

Matthew R MillerWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca NY 14850.
David J McDermittWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca NY 14850.
Cecile SauvanetWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca NY 14850.
Andrew T LombardoWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca NY 14850.
Riasat ZamanWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca NY 14850.
Anthony BretscherWeill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca NY 14850.
Cornell University · US

Funding

Microfilament Function in Cell PolarityR35GM131751 · NIGMS · CORNELL UNIVERSITY · PI BRETSCHER, ANTHONY P. · 2019 to 2022
$3.2M
NIGMS NIH HHS R35 GM131751
6 · The paper itself

Abstract

Here we report on the related TBC/RabGAPs EPI64A and EPI64B and show that they function to organize the apical aspect of epithelial cells. EPI64A binds the scaffolding protein EBP50/NHERF1, which itself binds active ezrin in epithelial cell microvilli. Epithelial cells additionally express EPI64B that also localizes to microvilli. However, EPI64B does not bind EBP50 and both proteins are shown to have a microvillar localization domain that spans the RabGAP domains. CRISPR/Cas9 was used to inactivate expression of each protein individually or both in Jeg-3 and Caco2 cells. In Jeg-3 cells, loss of EPI64B resulted in a reduction of apical microvilli, and a further reduction was seen in the double knockout, mostly likely due to misregulation of Rab8 and Rab35. In addition, apical junctions were partially disrupted in cells lacking EPI64A and accentuated in the double knockout. In Caco2 loss of EPI64B resulted in wavy junctions, whereas loss of both EPI64A and EPI64B had a severe phenotype often resulting in cells with a stellate apical morphology. In the knockout cells, the basal region of the cell remained unchanged, so EPI64A and EPI64B specifically localize to and regulate the morphology of the apical domain of polarized epithelial cells.

Indexed as

Adaptor Proteins, Signal TransducingBinding SitesCaco-2 CellsCell Line, TumorCell PolarityCytoskeletal ProteinsEpithelial CellsEzrinGTPase-Activating ProteinsHumansMicrovilliPhosphoproteinsPhosphorylationProtein BindingAdaptor Proteins, Signal TransducingCytoskeletal ProteinsEzrinGTPase-Activating ProteinsPhosphoproteinsTBC1D10A protein, humanTBC1D10B protein, human

Identifiers

PMID34757852
PMCPMC8886810
OpenAlexW3211735019

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.