ArticleThe EMBO journal2016
Phosphorylation-dependent Akt-Inversin interaction at the basal body of primary cilia.
Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.
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Who cites it
43 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.
- Analysis from the perspective of cilia: the protective effect of PARP inhibitors on visual function during light-induced damage.International ophthalmology · 2020Pooled it
- Suppression of Ciliogenesis Alleviates Cellular Senescence via AKT Signaling in Gingival Aging.Aging cell · 2026Article
- Primary cilia and cancer: a tale of many faces.Oncogene · 2025Review
- NEK8, a NIMA-family protein kinase at the core of the ciliary INV complex.Cell communication and signaling : CCS · 2025Review
- The Primary Cilia are Associated with the Axon Initial Segment in Neurons.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Review
- SLMAP3 is crucial for organogenesis through mechanisms involving primary cilia formation.Open biology · 2024Article
- The implication of ciliary signaling pathways for epithelial-mesenchymal transition.Molecular and cellular biochemistry · 2024Review
- Phosphoinositides in New Spaces.Cold Spring Harbor perspectives in biology · 2023Review
- Enhanced primary ciliogenesis via mitochondrial oxidative stress activates AKT to prevent neurotoxicity in HSPA9/mortalin-depleted SH-SY5Y cells.Molecular brain · 2023Article
- Cholesterol and Phosphoinositides in Cilia Biology.Advances in experimental medicine and biology · 2023Review
- Primary Cilia Restrain PI3K-AKT Signaling to Orchestrate Human Decidualization.International journal of molecular sciences · 2022Article
- The Role of Primary Cilia-Associated Phosphoinositide Signaling in Development.Journal of developmental biology · 2022Review
- Proteomic Profiling of Plasma-Derived Biomarkers in Patients with Bladder Cancer: A Step towards Clinical Translation.Life (Basel, Switzerland) · 2021Article
- Cep55 regulation of PI3K/Akt signaling is required for neocortical development and ciliogenesis.PLoS genetics · 2021Article
- Targeting Pin1 renders pancreatic cancer eradicable by synergizing with immunochemotherapy.Cell · 2021Article
- A complement factor H homolog, heparan sulfation, and syndecan maintain inversin compartment boundaries inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- DNA damage promotes microtubule dynamics through a DNA-PK-AKT axis for enhanced repair.The Journal of cell biology · 2021Article
- The essential role of primary cilia in cerebral cortical development and disorders.Current topics in developmental biology · 2021Review
- Superresolution Microscopy Reveals Distinct Phosphoinositide Subdomains Within the Cilia Transition Zone.Frontiers in cell and developmental biology · 2021Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A primary cilium is a microtubule-based sensory organelle that plays an important role in human development and disease. However, regulation of Akt in cilia and its role in ciliary development has not been demonstrated. Using yeast two-hybrid screening, we demonstrate that Inversin (INVS) interacts with Akt. Mutation in the INVS gene causes nephronophthisis type II (NPHP2), an autosomal recessive chronic tubulointerstitial nephropathy. Co-immunoprecipitation assays show that Akt interacts with INVS via the C-terminus. In vitro kinase assays demonstrate that Akt phosphorylates INVS at amino acids 864-866 that are required not only for Akt interaction, but also for INVS dimerization. Co-localization of INVS and phosphorylated form of Akt at the basal body is augmented by PDGF-AA Akt-null MEF cells as well as siRNA-mediated inhibition of Akt attenuated ciliary growth, which was reversed by Akt reintroduction. Mutant phosphodead- or NPHP2-related truncated INVS, which lack Akt phosphorylation sites, suppress cell growth and exhibit distorted lumen formation and misalignment of spindle axis during cell division. Further studies will be required for elucidating functional interactions of Akt-INVS at the primary cilia for identifying the molecular mechanisms underlying NPHP2.
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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.