Abstract
THE LIM homeodomain (LIM-HD) proteins, which contain two tandem LIM domains followed by a homeodomain, are critical transcriptional regulators of embryonic development1–5. The LIM domain is a conserved cysteine-rich zinc-binding motif found in LIM-HD and LMO (rhombotin or Ttg) proteins, cytoskeletal components, LIM kinases and other proteins1. LIM domains are protein-protein interaction motifs1, can inhibit binding of LIM-HD proteins to DNA6,7 and can negatively regulate LIM-HD protein function8. How LIM domains exert these regulatory effects is not known. We have now isolated a new LIM-domain-binding factor, Ldbl, on the basis of its ability to interact with the LIM-HD protein Lhxl (Liml) 9. High-affinity binding by Ldbl requires paired LIM domains and is restricted to the related subgroup of LIM domains found in LIM-HD and LMO proteins. The highly conserved Xenopus Ldb protein XLdbl, interacts with Xlim-1, the Xenopus orthologue of Lhxl. When injected into Xenopus embryos, XLdbl (or Ldbl) can synergize with Xlim-1 in the formation of partial secondary axes and in activation of the genes encoding goosecoid (gsc), chordin, NCAM and XCG7, demonstrating a functional as well as a physical interaction between the two proteins.
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Agulnick, A., Taira, M., Breen, J. et al. Interactions of the LIM-domain-binding factor Ldbl with LIM homeodomain proteins. Nature 384, 270–272 (1996). https://doi.org/10.1038/384270a0
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DOI: https://doi.org/10.1038/384270a0
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