Evidence map›Paper›PMID 34188035›Full record

ArticleNature communications2021

Structural mechanism of laminin recognition by integrin.

Takao Arimori, Naoyuki Miyazaki, Emiko Mihara, Mamoru Takizawa, Yukimasa Taniguchi, Carlos Cabañas, Kiyotoshi Sekiguchi, Junichi Takagi

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
8.0field-weighted citation impact, top 1% 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

66 citing papers in PubMed, 100 citations in OpenAlex.

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6 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Takao ArimoriLaboratory for Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.ORCID http://orcid.org/0000-0002-6063-5572
Naoyuki MiyazakiLaboratory for Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.ORCID http://orcid.org/0000-0002-4880-7300
Emiko MiharaLaboratory for Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.ORCID http://orcid.org/0000-0002-9127-8643
Mamoru TakizawaDivision of Matrixome Research and Application, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
Yukimasa TaniguchiDivision of Matrixome Research and Application, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
Carlos CabañasCell-cell Communication & Inflammation Unit, Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Madrid, Spain.ORCID http://orcid.org/0000-0002-8767-060X
Kiyotoshi SekiguchiDivision of Matrixome Research and Application, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
Junichi TakagiLaboratory for Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka, Japan. takagi@protein.osaka-u.ac.jp.ORCID http://orcid.org/0000-0002-1219-475X
Protein Research Foundation · JPUniversidad Complutense de Madrid · ESUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recognition of laminin by integrin receptors is central to the epithelial cell adhesion to basement membrane, but the structural background of this molecular interaction remained elusive. Here, we report the structures of the prototypic laminin receptor α6β1 integrin alone and in complex with three-chain laminin-511 fragment determined via crystallography and cryo-electron microscopy, respectively. The laminin-integrin interface is made up of several binding sites located on all five subunits, with the laminin γ1 chain C-terminal portion providing focal interaction using two carboxylate anchor points to bridge metal-ion dependent adhesion site of integrin β1 subunit and Asn189 of integrin α6 subunit. Laminin α5 chain also contributes to the affinity and specificity by making electrostatic interactions with large surface on the β-propeller domain of α6, part of which comprises an alternatively spliced X1 region. The propeller sheet corresponding to this region shows unusually high mobility, suggesting its unique role in ligand capture.

Indexed as

Amino Acid SequenceBasement MembraneBinding SitesCell AdhesionCryoelectron MicroscopyCrystallography, X-RayEpithelial CellsHumansIntegrin alpha6Integrin alpha6beta1Integrin beta1LamininProtein ConformationProtein DomainsStatic ElectricityIntegrin alpha6Integrin alpha6beta1Integrin beta1Lamininlaminin alpha5laminin gamma 1

Identifiers

PMID34188035
PMCPMC8241838
OpenAlexW3174920566

What OpenQuestion holds

Textmetadata
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.