Evidence map›Paper›PMID 29428502›Full record

ArticleBiochimica et biophysica acta. Biomembranes2018

Protein 4.1N is required for the formation of the lateral membrane domain in human bronchial epithelial cells.

Yaomei Wang, Huizhen Zhang, Qiaozhen Kang, Jing Liu, Haibo Weng, Wei Li, Narla Mohandas, Xiuli An, Lixiang Chen

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Review
  3. Identification and Functional Analysis of EPORJournal of immunology research · 2020
    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

9 authors at 4 institutions in 2 countries.

Yaomei WangSchool of Life Sciences, Zhengzhou University, Zhengzhou 450001, China.
Huizhen ZhangCollege of Public Health, Zhengzhou University, Zhengzhou 450001, China.
Qiaozhen KangSchool of Life Sciences, Zhengzhou University, Zhengzhou 450001, China.
Jing LiuThe State Key Laboratory of Medical Genetics, School of Life Sciences, Central South University, Changsha 410078, China.
Haibo WengSchool of Life Sciences, Zhengzhou University, Zhengzhou 450001, China.
Wei LiSchool of Life Sciences, Zhengzhou University, Zhengzhou 450001, China; Department of Immunology, the Affiliated Cancer Hospital of Zhengzhou University, Henan Cancer Hospital, Zhengzhou 450008, China.
Narla MohandasRed Cell Physiology Laboratory, New York Blood Center, New York, NY 10065, United States.
Xiuli AnSchool of Life Sciences, Zhengzhou University, Zhengzhou 450001, China; Laboratory of Membrane Biology, New York Blood Center, New York, NY 10065, United States. Electronic address: xan@nybc.org.
Lixiang ChenSchool of Life Sciences, Zhengzhou University, Zhengzhou 450001, China. Electronic address: lxchen@zzu.edu.cn.
Zhengzhou University · CNCentral South University · CNHenan Cancer Hospital · CNNew York Blood Center · US

Funding

RED CELL DEFORMABILITY IN VITRO AND SURVIVAL IN VIVOR37DK026263 · NIDDK · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI NARLA, MOHANDAS · 1995 to 2017
$4.5M
RED CELL DEFORMABILITY IN VITRO AND SURVIVAL IN VIVOR01DK026263 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1986 to 2007
$1.6M
TET3 in Terminal Erythroid DifferentiationR01DK100810 · NIDDK · NEW YORK BLOOD CENTER · PI AN, XIULI · 2014 to 2016
$875k
NIDDK NIH HHS R01 DK026263NIDDK NIH HHS R01 DK100810NIDDK NIH HHS R37 DK026263NIH HHS DK100810NIH HHS DK26263
6 · The paper itself

Abstract

The membrane skeleton forms a scaffold on the cytoplasmic side of the plasma membrane. The erythrocyte membrane represents an archetype of such structural organization. It has been documented that a similar membrane skeleton also exits in the Golgi complex. It has been previously shown that βII spectrin and ankyrin G are localized at the lateral membrane of human bronchial epithelial cells. Here we show that protein 4.1N is also located at the lateral membrane where it associates E-cadherin, β-catenin and βII spectrin. Importantly, depletion of 4.1N by RNAi in human bronchial epithelial cells resulted in decreased height of lateral membrane, which was reversed following re-expression of mouse 4.1N. Furthermore, although the initial phase of lateral membrane biogenesis proceeded normally in 4.1N-depleted cells, the final height of the lateral membrane of 4.1N-depleted cells was shorter compared to that of control cells. Our findings together with previous findings imply that 4.1N, βII spectrin and ankyrin G are structural components of the lateral membrane skeleton and that this skeleton plays an essential role in the assembly of a fully functional lateral membrane.

Indexed as

AnimalsBronchiCell CommunicationCell MembraneCells, CulturedCytoskeletal ProteinsEpithelial CellsHumansMembrane MicrodomainsMembrane ProteinsMiceNeuropeptidesRespiratory MucosaCytoskeletal Proteinserythrocyte membrane protein band 4.1-like 1Membrane ProteinsNeuropeptidesHuman bronchial epithelial cellsLateral membraneProtein 4.1N

Identifiers

PMID29428502
PMCPMC7335216
OpenAlexW2792908392

What OpenQuestion holds

Textmetadata
LicenceTDM
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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.