ArticleThe EMBO journal2007
The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 66 citations in OpenAlex.
- Oligomerization and positive feedback on membrane recruitment encode dynamically stable PAR-3 asymmetries in thebioRxiv : the preprint server for biology · 2025Article
- TMEM25 is a Par3-binding protein that attenuates claudin assembly during tight junction development.EMBO reports · 2024Article
- Design principles for selective polarization of PAR proteins by cortical flows.The Journal of cell biology · 2023Article
- Anomalous Oligomerization Behavior ofInternational journal of molecular sciences · 2023Article
- Structural Organization of Human Full-Length PAR3 and the aPKC-PAR6 Complex.Molecular biotechnology · 2022Article
- Head-to-tail polymerization by VEL proteins underpins cold-induced Polycomb silencing in flowering control.Cell reports · 2022Article
- Apical-basal polarity and the control of epithelial form and function.Nature reviews. Molecular cell biology · 2022Review
- The Roles of Par3, Par6, and aPKC Polarity Proteins in Normal Neurodevelopment and in Neurodegenerative and Neuropsychiatric Disorders.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Review
- Par-3 family proteins in cell polarity & adhesion.The FEBS journal · 2022Review
- Going with the flow: insights fromPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Review
- Par complex cluster formation mediated by phase separation.Nature communications · 2020Article
- Structural Features of Tight-Junction Proteins.International journal of molecular sciences · 2019Review
- Switching states: dynamic remodelling of polarity complexes as a toolkit for cell polarization.Current opinion in cell biology · 2019Review
- Reconstruction of Par-dependent polarity in apolar cells reveals a dynamic process of cortical polarization.eLife · 2019Article
- Redundant regulation of localization and protein stability of DmPar3.Cellular and molecular life sciences : CMLS · 2018Article
- PAR3-PAR6-atypical PKC polarity complex proteins in neuronal polarization.Cellular and molecular life sciences : CMLS · 2018Review
- The PAR proteins: from molecular circuits to dynamic self-stabilizing cell polarity.Development (Cambridge, England) · 2017Review
- aPKC Cycles between Functionally Distinct PAR Protein Assemblies to Drive Cell Polarity.Developmental cell · 2017Article
- A Single-Cell Biochemistry Approach Reveals PAR Complex Dynamics during Cell Polarization.Developmental cell · 2017Article
- Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.Nature communications · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The evolutionarily conserved Par-3/Par-6/aPKC complex is essential for the establishment and maintenance of polarity of a wide range of cells. Both Par-3 and Par-6 are PDZ domain containing scaffold proteins capable of binding to polarity regulatory proteins. In addition to three PDZ domains, Par-3 also contains a conserved N-terminal oligomerization domain (NTD) that is essential for proper subapical membrane localization and consequently the functions of Par-3. The molecular basis of NTD-mediated Par-3 membrane localization is poorly understood. Here, we describe the structure of a monomeric form of the Par-3 NTD. Unexpectedly, the domain adopts a PB1-like fold with both type-I and type-II structural features. The Par-3 NTD oligomerizes into helical filaments via front-to-back interactions. We further demonstrate that the NTD-mediated membrane localization of Par-3 in MDCK cells is solely attributed to its oligomerization capacity. The data presented in this study suggest that the Par-3 NTD is likely to facilitate the assembly of higher-order Par-3/Par-6/aPKC complex with increased avidities in targeting the complex to the subapical membrane domain and in binding to other polarity-regulating proteins.
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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.