Dev Biol 2024 Nov 01;515:46-58. doi: 10.1016/j.ydbio.2024.06.022.

Reversion induced LIM domain protein (RIL) is a Daam1-interacting protein and regulator of the actin cytoskeleton during non-canonical Wnt signaling.

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The Daam1 protein regulates Wnt-induced cytoskeletal changes during vertebrate gastrulation though its full mode of action and binding partners remain unresolved. Here we identify Reversion Induced LIM domain protein (RIL) as a new interacting protein of Daam1. Interaction studies uncover binding of RIL to the C-terminal actin-nucleating portion of Daam1 in a Wnt-responsive manner. Immunofluorescence studies showed subcellular localization of RIL to actin fibers and co-localization with Daam1 at the plasma membrane. RIL gain- and loss-of-function approaches in Xenopus produced severe gastrulation defects in injected embryos. Additionally, a simultaneous loss of Daam1 and RIL synergized to produce severe gastrulation defects indicating RIL and Daam1 may function in the same signaling pathway. RIL further synergizes with another novel Daam1-interacting protein, Formin Binding Protein 1 (FNBP1), to regulate gastrulation. Our studies altogether show RIL mediates Daam1-regulated non-canonical Wnt signaling that is required for vertebrate gastrulation.

???displayArticle.pubmedLink??? 38968989
???displayArticle.pmcLink??? PMC11321505
???displayArticle.link??? Dev Biol
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Species referenced: Xenopus Xenopus laevis
Genes referenced: acta2 actn1 chrd ctnnb1 daam1 dvl2 fmn1 fnbp1 gsc myc pdlim4 rho tbxt wnt3a wnt5a wnt8a
GO keywords: plasma membrane [+]
???displayArticle.antibodies??? Myc Ab13 Myc Ab19
???displayArticle.morpholinos??? daam1 MO1 fnbp1 MO2 fnbp1 MO3

???displayArticle.disOnts??? neural tube defect