ArticleThe FEBS journal2026
Structural and functional dissection of the WH2/DAD motif of INF2, a formin linked to human inherited degenerative disorders.
Article in The FEBS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- An INF2-dependent actin-mediated step in inositol 1,4,5-trisphosphate receptor cluster formation and activity.Current biology : CB · 2026Article
- ERM proteins support perinuclear actin rim formation.Frontiers in cell and developmental biology · 2025Article
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6 authors.
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Abstract
Inverted formin-2 (INF2), a formin linked to inherited renal and neurological disorders, exhibits pathogenic variants that lead to deregulated actin polymerization and nuclear aberrations, ultimately compromising cell viability. Most formins contain a diaphanous autoregulatory domain (DAD) and a diaphanous inhibitory domain (DID), which interact to keep the molecule in an inactive state. The DAD consists of a short sequence with an N-terminal region rich in hydrophobic residues and a C-terminal segment abundant in basic residues, resembling WASP homology 2 (WH2) actin-binding domains. Based on its sequence and actin-binding ability, the DAD of INF2 qualifies as a WH2 motif. In this study, we investigated the structure of the INF2 WH2/DAD by nuclear magnetic resonance (NMR) and explored its functional role. Our analysis revealed that the WH2/DAD forms a single α-helix in both H
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