ArticleeLife2022
Super-resolution imaging uncovers the nanoscopic segregation of polarity proteins in epithelia.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Bulk delivery of a preassembled apical surface initiates epithelial lumen formation.Nature communications · 2026Article
- Tight junction structure, assembly and (dys)function.Nature reviews. Molecular cell biology · 2026Review
- Loss of intermicrovillar adhesion factor CDHR2 impairs basolateral junctional complexes in transporting epithelia.Molecular biology of the cell · 2024Article
- Protein droplets spread to seal tight junctions.Nature · 2024Article
- Article
- A neuroligin-2-YAP axis regulates progression of pancreatic intraepithelial neoplasia.EMBO reports · 2024Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Apical PAR-3 caps orient the mitotic spindle inbioRxiv : the preprint server for biology · 2023Article
- The polarity protein PARD3 and cancer.Oncogene · 2021Review
- The Nanoscopic Organization of Synapse Structures: A Common Basis for Cell Communication.Membranes · 2021Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Epithelial tissues acquire their integrity and function through the apico-basal polarization of their constituent cells. Proteins of the PAR and Crumbs complexes are pivotal to epithelial polarization, but the mechanistic understanding of polarization is challenging to reach, largely because numerous potential interactions between these proteins and others have been found, without a clear hierarchy in importance. We identify the regionalized and segregated organization of members of the PAR and Crumbs complexes at epithelial apical junctions by imaging endogenous proteins using stimulated-emission-depletion microscopy on Caco-2 cells, and human and murine intestinal samples. Proteins organize in submicrometric clusters, with PAR3 overlapping with the tight junction (TJ) while PALS1-PATJ and aPKC-PAR6β form segregated clusters that are apical of the TJ and present in an alternated pattern related to actin organization. CRB3A is also apical of the TJ and partially overlaps with other polarity proteins. Of the numerous potential interactions identified between polarity proteins, only PALS1-PATJ and aPKC-PAR6β are spatially relevant in the junctional area of mature epithelial cells, simplifying our view of how polarity proteins could cooperate to drive and maintain cell polarity.
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What OpenQuestion holds
Registered trials
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.