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Updated: Jun 11, 2026

Evaluation of Planar-Cell-Polarity Phenotypes in Ciliopathy Mouse Mutant Cochlea
Published on: February 21, 2016
ASPP2 regulates epithelial cell polarity through the PAR complex.
Weili Cong1, Tomonori Hirose, Yutaka Harita
1Department of Molecular Biology, Yokohama City University Graduate School of Medical Science, 3-9 Fuku-ura, Kanazawa-ku, Yokohama, Japan.
Apoptosis-stimulating protein of p53 (ASPP2) regulates epithelial cell polarity by interacting with the PAR complex. ASPP2 and PAR-3 cooperate to maintain cell polarity and tissue integrity.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The PAR complex (PAR-3, PAR-6, aPKC) is crucial for cell polarity in epithelial cells.
- Regulatory mechanisms governing PAR complex function are not fully understood.
- Apoptosis-stimulating protein of p53 (ASPP2) interacts with p53 and promotes apoptosis.
Purpose of the Study:
- To investigate the role of ASPP2 in regulating epithelial cell polarity.
- To elucidate the interaction between ASPP2 and the PAR complex.
Main Methods:
- Immunofluorescence microscopy to assess protein localization.
- Depletion studies (e.g., siRNA) to evaluate the function of ASPP2 and PAR-3.
- Analysis of tight junction formation and apical membrane domain development.
Main Results:
- ASPP2 interacts and colocalizes with PAR-3 at apical junctions in polarized epithelial cells.
- Depletion of ASPP2 disrupts cell polarity, tight junctions, and apical domain maintenance.
- ASPP2 depletion affects PAR-3 localization, and vice versa, indicating a cooperative relationship.
- Disruption of ASPP2-PAR-3 interaction impairs cell polarity.
Conclusions:
- ASPP2 positively regulates epithelial cell polarity by associating with the PAR complex, specifically PAR-3.
- ASPP2 and PAR-3 cooperate to form an active PAR complex, essential for maintaining cell polarity.
- ASPP2 links cell polarity regulation with other cellular processes it mediates.
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