Evidence map›Paper›PMID 30404858›Full record

ArticleMolecular & cellular proteomics : MCP2019

Assembly of the β4-Integrin Interactome Based on Proximal Biotinylation in the Presence and Absence of Heterodimerization.

Satu-Marja Myllymäki, Ulla-Reetta Kämäräinen, Xiaonan Liu, Sara Pereira Cruz, Sini Miettinen, Mikko Vuorela, Markku Varjosalo, Aki Manninen

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

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  4. Phagocytosis by the retinal pigment epithelium: New insights into polarized cell mechanics.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
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  11. Article
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  13. Article
  14. Frontiers in immunology · 2020
    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 2 institutions in 1 country.

Satu-Marja MyllymäkiOulu Center for Cell-Matrix Research, Biocenter Oulu, Faculty of Biochemistry and Molecular Medicine, University of Oulu, Finland;. Electronic address: satu-marja.myllymaki@helsinki.fi.
Ulla-Reetta KämäräinenOulu Center for Cell-Matrix Research, Biocenter Oulu, Faculty of Biochemistry and Molecular Medicine, University of Oulu, Finland.
Xiaonan LiuInstitute of Biotechnology and Helsinki Institute of Life Science, University of Helsinki, Helsinki, Finland.
Sara Pereira CruzOulu Center for Cell-Matrix Research, Biocenter Oulu, Faculty of Biochemistry and Molecular Medicine, University of Oulu, Finland.
Sini MiettinenInstitute of Biotechnology and Helsinki Institute of Life Science, University of Helsinki, Helsinki, Finland.
Mikko VuorelaOulu Center for Cell-Matrix Research, Biocenter Oulu, Faculty of Biochemistry and Molecular Medicine, University of Oulu, Finland.
Markku VarjosaloInstitute of Biotechnology and Helsinki Institute of Life Science, University of Helsinki, Helsinki, Finland.
Aki ManninenOulu Center for Cell-Matrix Research, Biocenter Oulu, Faculty of Biochemistry and Molecular Medicine, University of Oulu, Finland;. Electronic address: aki.manninen@oulu.fi.
University of Oulu · FIUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrin-mediated laminin adhesions mediate epithelial cell anchorage to basement membranes and are critical regulators of epithelial cell polarity. Integrins assemble large multiprotein complexes that link to the cytoskeleton and convey signals into the cells. Comprehensive proteomic analyses of actin network-linked focal adhesions (FA) have been performed, but the molecular composition of intermediate filament-linked hemidesmosomes (HD) remains incompletely characterized. Here we have used proximity-dependent biotin identification (BioID) technology to label and characterize the interactome of epithelia-specific β4-integrin that, as α6β4-heterodimer, forms the core of HDs. The analysis identified ∼150 proteins that were specifically labeled by BirA-tagged integrin-β4. In addition to known HDs proteins, the interactome revealed proteins that may indirectly link integrin-β4 to actin-connected protein complexes, such as FAs and dystrophin/dystroglycan complexes. The specificity of the screening approach was validated by confirming the HD localization of two candidate β4-interacting proteins, utrophin (UTRN) and ELKS/Rab6-interacting/CAST family member 1 (ERC1). Interestingly, although establishment of functional HDs depends on the formation of α6β4-heterodimers, the assembly of β4-interactome was not strictly dependent on α6-integrin expression. Our survey to the HD interactome sets a precedent for future studies and provides novel insight into the mechanisms of HD assembly and function of the β4-integrin.

Indexed as

AnimalsBiotinylationChromatography, LiquidDogsIntegrin beta4Madin Darby Canine Kidney CellsProtein Interaction MapsProtein MultimerizationProteomicsTandem Mass SpectrometryIntegrin beta4BioIDCell AdhesionEpitheliumExtracellular MatrixHemidesmosomeIntegrinKidney Function or BiologyMass SpectrometryProtein Complex Analysis

Identifiers

PMID30404858
PMCPMC6356083
OpenAlexW2900121162

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.