ArticleScientific reports2019
Vangl2 interaction plays a role in the proteasomal degradation of Prickle2.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Article
- PRICKLE3 protects VANGL proteins from CK1-mediated phosphorylation and RNF43-mediated degradation.Communications biology · 2025Article
- Evolving Insights into Prickle2 in Neurodevelopment and Neurological Disorders.Molecular neurobiology · 2025Review
- Cryo-EM structure and oligomerization of the human planar cell polarity core protein Vangl1.Nature communications · 2025Article
- Decoding Epilepsy: Prickle2 and Multifaceted Molecular Pathway Connections.Current pharmaceutical design · 2025Review
- Article
- Planar Cell Polarity Signaling: Coordinated Crosstalk for Cell Orientation.Journal of developmental biology · 2024Review
- Functional interaction between Vangl2 and N-cadherin regulates planar cell polarization of the developing neural tube and cochlear sensory epithelium.Scientific reports · 2023Article
- Distinct overlapping functions for Prickle1 and Prickle2 in the polarization of the airway epithelium.Frontiers in cell and developmental biology · 2022Article
- Vangl as a Master Scaffold for Wnt/Planar Cell Polarity Signaling in Development and Disease.Frontiers in cell and developmental biology · 2022Review
- Prickle promotes the formation and maintenance of glutamatergic synapses by stabilizing the intercellular planar cell polarity complex.Science advances · 2021Article
- Molecular mechanisms mediating asymmetric subcellular localisation of the core planar polarity pathway proteins.Biochemical Society transactions · 2020Review
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The PET and LIM domain-containing protein, Prickle, plays a key role in planar cell polarity (PCP) in Drosophila. It has been reported that mutations in the PRICKLE2 gene, which encodes one of the human orthologues of Prickle, are associated with human diseases such as epilepsy and autism spectrum disorder. To develop preventive and therapeutic strategies for these intractable diseases, we studied the regulation of Prickle2 protein levels in transfected HEK293T cells. Prickle2 levels were negatively regulated by a physical interaction with another PCP protein, Van Gogh-like 2 (Vangl2). The Vangl2-mediated reduction in Prickle2 levels was, at least in part, relieved by proteasome inhibitors or by functional inhibition of the Cullin-1 E3 ubiquitin ligase. Furthermore, the expression of Vangl2 enhanced the polyubiquitination of Prickle2. This ubiquitination was partially blocked by co-expression of a ubiquitin mutant, which cannot be polymerised through their Lys48 residue to induce target proteins toward proteasomal degradation. Together, these results suggest that Prickle2 is polyubiquitinated by the Vangl2 interaction in a Cullin-1-dependent manner to limit its expression levels. This regulation may play a role in the local and temporal fine-tuning of Prickle protein levels during PCP signal-dependent cellular behaviours.
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