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Letters to Nature
Nature 384, 270 - 272 (21 November 1996); doi:10.1038/384270a0

Interactions of the LIM-domain-binding factor Ldbl with LIM homeodomain proteins

Alan D. Agulnick, Masanori Taira*, Joseph J. Breen*, Tomohiro Tanaka*, Igor B. Dawid* & Heiner Westphal

Laboratory of Mammalian Genes and Development, * Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA
Present address: Laboratory of Molecular Embryology, Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan

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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