ArticleBiochemistry2016
Binding of Crumbs to the Par-6 CRIB-PDZ Module Is Regulated by Cdc42.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 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
22 citing papers in PubMed.
- LGL-1 and the RhoGAP protein PAC-1 redundantly polarize thebioRxiv : the preprint server for biology · 2026Article
- Dorsal forerunner cells transmit epiboly forces to extend the zebrafish notochord.bioRxiv : the preprint server for biology · 2025Article
- A PAR6-aPKC-LGL structure reveals how LGL antagonizes aPKC.Nature structural & molecular biology · 2025Article
- Capture, mutual inhibition and release mechanism for aPKC-Par6 and its multisite polarity substrate Lgl.Nature structural & molecular biology · 2025Article
- A PDZ-kinase allosteric relay mediates Par complex regulator exchange.bioRxiv : the preprint server for biology · 2024Article
- Human CRB1 and CRB2 form homo- and heteromeric protein complexes in the retina.Life science alliance · 2024Article
- The Cyst Epithelium in Polycystic Kidney Disease Patients Displays Normal Apical-Basolateral Cell Polarity.International journal of molecular sciences · 2024Article
- Allosteric Signaling in PDZ Energetic Networks: Embedding Error Analysis.The journal of physical chemistry. B · 2023Article
- Apical-basal polarity and the control of epithelial form and function.Nature reviews. Molecular cell biology · 2022Review
- Pak1 and PP2A antagonize aPKC function to support cortical tension induced by the Crumbs-Yurt complex.eLife · 2021Article
- RhoGAP19D inhibits Cdc42 laterally to control epithelial cell shape and prevent invasion.The Journal of cell biology · 2021Article
- Mechanoregulation of PDZ Proteins, An Emerging Function.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Article
- Research Models and Gene Augmentation Therapy forFrontiers in neuroscience · 2020Review
- Phospholipids of the Plasma Membrane - Regulators or Consequence of Cell Polarity?Frontiers in cell and developmental biology · 2020Review
- Structural Features of Tight-Junction Proteins.International journal of molecular sciences · 2019Review
- Cdc42 defines apical identity and regulates epithelial morphogenesis by promoting apical recruitment of Par6-aPKC and Crumbs.Development (Cambridge, England) · 2019Article
- Emerging Themes in PDZ Domain Signaling: Structure, Function, and Inhibition.International review of cell and molecular biology · 2019Review
- Regulation of Cell Polarity by Exocyst-Mediated Trafficking.Cold Spring Harbor perspectives in biology · 2018Review
- The Crumbs3 Polarity Protein.Cold Spring Harbor perspectives in biology · 2018Review
Corrections and comments
- Erratum issued
Authors and funding
6 authors.
Funding
Abstract
Par-6 is a scaffold protein that organizes other proteins into a complex required to initiate and maintain cell polarity. Cdc42-GTP binds the CRIB module of Par-6 and alters the binding affinity of the adjoining PDZ domain. Allosteric regulation of the Par-6 PDZ domain was first demonstrated using a peptide identified in a screen of typical carboxyl-terminal ligands. Crumbs, a membrane protein that localizes a conserved polarity complex, was subsequently identified as a functional partner for Par-6 that likely interacts with the PDZ domain. Here we show by nuclear magnetic resonance that Par-6 binds a Crumbs carboxyl-terminal peptide and report the crystal structure of the PDZ-peptide complex. The Crumbs peptide binds Par-6 more tightly than the previously studied carboxyl peptide ligand and interacts with the CRIB-PDZ module in a Cdc42-dependent manner. The Crumbs:Par-6 crystal structure reveals specific PDZ-peptide contacts that contribute to its higher affinity and Cdc42-enhanced binding. Comparisons with existing structures suggest that multiple C-terminal Par-6 ligands respond to a common conformational switch that transmits the allosteric effects of GTPase binding.
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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.