Evidence map›Paper›PMID 36764939›Full record

ArticleCell and tissue research2023

LRP2 contributes to planar cell polarity-dependent coordination of motile cilia function.

Lena Bunatyan, Anca Margineanu, Camille Boutin, Mireille Montcouquiol, Sebastian Bachmann, Erik Ilsø Christensen, Thomas E Willnow, Annabel Christ

Open access · hybridAbstract read
In one paragraph

Article in Cell and tissue research, 2023. 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
1.3field-weighted citation impact, top 18% 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, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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

8 authors at 5 institutions in 3 countries.

Lena BunatyanMax-Delbrueck-Center for Molecular Medicine, Robert-Roessle-Str. 10, 13125, Berlin, Germany.
Anca MargineanuMax-Delbrueck-Center for Molecular Medicine, Robert-Roessle-Str. 10, 13125, Berlin, Germany.
Camille BoutinAix-Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.
Mireille MontcouquiolINSERM, Neurocentr Magendie, 33000, Bordeaux, France.
Sebastian BachmannInstitute for Vegetative Anatomy, Charité University Medicine Berlin, 10117, Berlin, Germany.
Erik Ilsø ChristensenDepartment of Biomedicine, Aarhus University, 8000, Aarhus, Denmark.
Thomas E WillnowMax-Delbrueck-Center for Molecular Medicine, Robert-Roessle-Str. 10, 13125, Berlin, Germany.
Annabel ChristMax-Delbrueck-Center for Molecular Medicine, Robert-Roessle-Str. 10, 13125, Berlin, Germany. annabel.christ@mdc-berlin.de.ORCID http://orcid.org/0000-0002-2019-176X
Max Delbrück Center · DEAarhus University · DKCentre National de la Recherche Scientifique · FRCharité - Universitätsmedizin Berlin · DEInserm · FR

Funding

Deutsche Forschungsgemeinschaft CH 1838/1-1
6 · The paper itself

Abstract

Motile cilia are protruding organelles on specialized epithelia that beat in a synchronous fashion to propel extracellular fluids. Coordination and orientation of cilia beating on individual cells and across tissues is a complex process dependent on planar cell polarity (PCP) signaling. Asymmetric sorting of PCP pathway components, essential to establish planar polarity, involves trafficking along the endocytic path, but the underlying regulatory processes remain incompletely understood. Here, we identified the endocytic receptor LRP2 as regulator of PCP component trafficking in ependyma, a multi-ciliated cell type that is involved in facilitating flow of the cerebrospinal fluid in the brain ventricular system. Lack of receptor expression in gene-targeted mice results in a failure to sort PCP core proteins to the anterior or posterior cell side and, consequently, in the inability to coordinate cilia arrangement and to aligned beating (loss of rotational and translational polarity). LRP2 deficiency coincides with a failure to sort NHERF1, a cytoplasmic LRP2 adaptor to the anterior cell side. As NHERF1 is essential to translocate PCP core protein Vangl2 to the plasma membrane, these data suggest a molecular mechanism whereby LRP2 interacts with PCP components through NHERF1 to control their asymmetric sorting along the endocytic path. Taken together, our findings identified the endocytic receptor LRP2 as a novel regulator of endosomal trafficking of PCP proteins, ensuring their asymmetric partition and establishment of translational and rotational planar cell polarity in the ependyma.

Indexed as

Cell PolarityCiliaAnimalsCarrier ProteinsCerebral VentriclesEpendymaLow Density Lipoprotein Receptor-Related Protein-2MiceWnt Signaling PathwayCarrier ProteinsLow Density Lipoprotein Receptor-Related Protein-2Lrp2 protein, mouseEndocytosisLRP2Motile ciliaNHERF1Planar cell polarity (PCP) signaling

Identifiers

PMID36764939
PMCPMC10172251
OpenAlexW4320032804

What OpenQuestion holds

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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.