Evidence map›Paper›PMID 39762628›Full record

ArticleNature structural & molecular biology2025

Capture, mutual inhibition and release mechanism for aPKC-Par6 and its multisite polarity substrate Lgl.

Christopher P Earl, Mathias Cobbaut, André Barros-Carvalho, Marina E Ivanova, David C Briggs, Eurico Morais-de-Sá, Peter J Parker, Neil Q McDonald

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. LGL-1 and the RhoGAP protein PAC-1 redundantly polarize thebioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. A PAR6-aPKC-LGL structure reveals how LGL antagonizes aPKC.Nature structural & molecular biology · 2025
    Article
  6. A PDZ-kinase allosteric relay mediates Par complex regulator exchange.bioRxiv : the preprint server for biology · 2024
    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

8 authors.

Christopher P Earl *Signalling and Structural Biology Laboratory, Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0002-9091-9955
Mathias Cobbaut *Signalling and Structural Biology Laboratory, Francis Crick Institute, London, UK. mathias.cobbaut@crick.ac.uk.ORCID http://orcid.org/0000-0003-0279-0336
André Barros-CarvalhoInstituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal.
Marina E IvanovaSignalling and Structural Biology Laboratory, Francis Crick Institute, London, UK.
David C BriggsSignalling and Structural Biology Laboratory, Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0002-9793-7339
Eurico Morais-de-SáInstituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal.ORCID http://orcid.org/0000-0003-3525-8231
Peter J ParkerProtein Phosphorylation Laboratory, Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0001-5907-6980
Neil Q McDonaldSignalling and Structural Biology Laboratory, Francis Crick Institute, London, UK. neil.mcdonald@crick.ac.uk.ORCID http://orcid.org/0000-0003-0975-6325

Funding

Wellcome Trust CC2068
6 · The paper itself

Abstract

The mutually antagonistic relationship of atypical protein kinase C (aPKC) and partitioning-defective protein 6 (Par6) with the substrate lethal (2) giant larvae (Lgl) is essential for regulating polarity across many cell types. Although aPKC-Par6 phosphorylates Lgl at three serine sites to exclude it from the apical domain, aPKC-Par6 and Lgl paradoxically form a stable kinase-substrate complex, with conflicting roles proposed for Par6. We report the structure of human aPKCι-Par6α bound to full-length Llgl1, captured through an aPKCι docking site and a Par6

Indexed as

Adaptor Proteins, Signal TransducingCell Cycle ProteinsProtein Kinase CTumor Suppressor ProteinsAnimalsCell PolarityCrystallography, X-RayHumansIsoenzymesModels, MolecularPhosphorylationProtein BindingProtein Kinase C-lambdaAdaptor Proteins, Signal TransducingCell Cycle ProteinsIsoenzymesPARD6A protein, humanPKC-3 proteinProtein Kinase CProtein Kinase C-lambdaTumor Suppressor Proteins

Identifiers

PMID39762628
PMCPMC11996676

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.