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. 2023 Jul 25;13:12003. doi: 10.1038/s41598-023-38588-7

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Locations of variants in the INF2 domain structure. The distribution of variants in INF2 functional domains is shown. Variants in exon 2 were found in individuals with a dual phenotype of Charcot–Marie–Tooth disease (CMT) and FSGS, whereas those in exon 3 and exon 4 were identified in patients with FSGS alone. INF2 is a large multi-domain protein composed of three functional domains: Diaphanous inhibitory domain (DID, orange), formin homology (FH) domains FH1 and FH2 (red and green), and diaphanous autoregulatory domain (DAD, blue). The DID interacts with the DAD within the same molecule (intramolecular autoinhibition) as well as with other actin regulators (e.g., small GTPase and mDia). The FH domains mediate both actin polymerization and depolymerization. Domain positions are according to UniprotKB-Q27J81. WH2: WASP homology 2; mDia: mammalian Diaphanous-related formin 1.