ArticleBioscience reports2016
Disease causing mutations in inverted formin 2 regulate its binding to G-actin, F-actin capping protein (CapZ α-1) and profilin 2.
Article in Bioscience reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Patient-specific hiPSC-Podocytes as an in vitro model of genetic FSGS.Scientific reports · 2025Article
- Autosomal dominant focal segmental glomerulosclerosis by INF2 p.Arg218Trp and p.Ser186Pro mutations: three case reports and literature review.BMC nephrology · 2025Review
- Regulation of formin INF2 and its alteration in INF2-linked inherited disorders.Cellular and molecular life sciences : CMLS · 2024Review
- INF2 formin variants linked to human inherited kidney disease reprogram the transcriptome, causing mitotic chaos and cell death.Cellular and molecular life sciences : CMLS · 2024Article
- Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry.International journal of molecular sciences · 2024Article
- Role of actin cytoskeleton in podocytes.Pediatric nephrology (Berlin, Germany) · 2021Review
- Review
- The formin INF2 in disease: progress from 10 years of research.Cellular and molecular life sciences : CMLS · 2020Review
- A Deregulated Stress Response Underlies Distinct INF2-Associated Disease Profiles.Journal of the American Society of Nephrology : JASN · 2020Article
- Capping Protein Insulates Arp2/3-Assembled Actin Patches from Formins.Current biology : CB · 2019Article
- TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility.Journal of the American Society of Nephrology : JASN · 2019Article
- Enhanced insulin receptor, but not PI3K, signalling protects podocytes from ER stress.Scientific reports · 2018Article
- Prolonged exposure of mouse and human podocytes to insulin induces insulin resistance through lysosomal and proteasomal degradation of the insulin receptor.Diabetologia · 2017Article
- Inverted formins: A subfamily of atypical formins.Cytoskeleton (Hoboken, N.J.) · 2017Review
- The Evolving Complexity of the Podocyte Cytoskeleton.Journal of the American Society of Nephrology : JASN · 2017Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Focal segmental glomerulosclerosis (FSGS) is a devastating form of nephrotic syndrome which ultimately leads to end stage renal failure (ESRF). Mutations in inverted formin 2 (INF2), a member of the formin family of actin-regulating proteins, have recently been associated with a familial cause of nephrotic syndrome characterized by FSGS. INF2 is a unique formin that can both polymerize and depolymerize actin filaments. How mutations in INF2 lead to disease is unknown. In the present study, we show that three mutations associated with FSGS, E184K, S186P and R218Q, reduce INF2 auto-inhibition and increase association with monomeric actin. Furthermore using a combination of GFP-INF2 expression in human podocytes and GFP-Trap purification coupled with MS we demonstrate that INF2 interacts with profilin 2 and the F-actin capping protein, CapZ α-1. These interactions are increased by the presence of the disease causing mutations. Since both these proteins are involved in the dynamic turnover and restructuring of the actin cytoskeleton these changes strengthen the evidence that aberrant regulation of actin dynamics underlies the pathogenesis of disease.
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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.