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Gene Review

Ldb1  -  LIM domain binding 1

Mus musculus

Synonyms: CLIM-2, CLIM2, Carboxyl-terminal LIM domain-binding protein 2, LDB-1, LIM domain-binding factor CLIM2, ...
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Disease relevance of Ldb1


High impact information on Ldb1

  • Using in vivo function and protein interaction assays, we found that Lhx3 binds directly to the LIM cofactor NLI to trigger V2 interneuron differentiation [4].
  • Whereas the isolated PKR kinase domain (KD) was non-functional in vivo, expression of a glutathione S-transferase-KD fusion, or co-expression of KD fusions containing the heterodimerization domains of the Xlim-1 and Ldb1 proteins, restored PKR activity in yeast cells [5].
  • This factor, referred to as LMO-4, is expressed in overlapping manner with Clim-2 in epidermis and in several other regions, including epithelial cells of the gastrointestinal, respiratory and genitourinary tracts, developing cartilage, pituitary gland, and discrete regions of the central and peripheral nervous system [6].
  • Forced expression of Ldb1 in G1ER proerythroblast cells inhibited cellular maturation, a finding compatible with the decrease in Ldb1 gene expression that normally occurs during erythroid differentiation [7].
  • These results suggest that Ssdp1 regulates the development of late head organizer tissues and body growth by functioning as an essential activator component of a Lim1 complex through interaction with Ldb1 [8].

Biological context of Ldb1


Anatomical context of Ldb1

  • In both the developing face and the limb buds we identify Fgf-8 as the likely candidate signalling molecule that regulates Clim-2 expression [13].
  • We show that in common with both these Lim genes, Clim-2 expression is regulated by signals from overlying epithelium [13].
  • In the mouse, embryonic expression of Clim-2 is particularly pronounced in facial ectomesenchyme and limb bud mesenchyme in association with Lim genes, Lhx-6 and Lmx-1 respectively [13].

Associations of Ldb1 with chemical compounds

  • Cofactor CLIM2 promotes the repressive action of LIM homeodomain transcription factor Lhx2 in the expression of porcine pituitary glycoprotein hormone alpha subunit gene [2].

Physical interactions of Ldb1


Other interactions of Ldb1

  • We have now identified a new member of the Lmo family, designated Lmo4, via its interaction with Ldb1 [9].
  • Cell proliferation is globally reduced in Ssdp1(hsk/hsk) mutants, and approximately half also exhibit smaller body size, similar to the phenotype observed in Lim1 and Ldb1 mutants [8].

Analytical, diagnostic and therapeutic context of Ldb1

  • The expression of CLIM2 gene in the anterior pituitary lobe was detected during the porcine fetal and postnatal period by RT-PCR analysis, suggesting that this protein is constitutively expressing and plays a basic role in the anterior pituitary [2].


  1. Identification of a TAL1 target gene reveals a positive role for the LIM domain-binding protein Ldb1 in erythroid gene expression and differentiation. Xu, Z., Huang, S., Chang, L.S., Agulnick, A.D., Brandt, S.J. Mol. Cell. Biol. (2003) [Pubmed]
  2. Cofactor CLIM2 promotes the repressive action of LIM homeodomain transcription factor Lhx2 in the expression of porcine pituitary glycoprotein hormone alpha subunit gene. Susa, T., Sato, T., Ono, T., Kato, T., Kato, Y. Biochim. Biophys. Acta (2006) [Pubmed]
  3. Liver-specific Ldb1 deletion results in enhanced liver cancer development. Teufel, A., Maass, T., Strand, S., Kanzler, S., Galante, T., Becker, K., Strand, D., Biesterfeld, S., Westphal, H., Galle, P.R. J. Hepatol. (2010) [Pubmed]
  4. LIM factor Lhx3 contributes to the specification of motor neuron and interneuron identity through cell-type-specific protein-protein interactions. Thaler, J.P., Lee, S.K., Jurata, L.W., Gill, G.N., Pfaff, S.L. Cell (2002) [Pubmed]
  5. Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR. Ung, T.L., Cao, C., Lu, J., Ozato, K., Dever, T.E. EMBO J. (2001) [Pubmed]
  6. Mouse deformed epidermal autoregulatory factor 1 recruits a LIM domain factor, LMO-4, and CLIM coregulators. Sugihara, T.M., Bach, I., Kioussi, C., Rosenfeld, M.G., Andersen, B. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  7. The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative regulators of erythroid differentiation. Visvader, J.E., Mao, X., Fujiwara, Y., Hahm, K., Orkin, S.H. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  8. Ssdp1 regulates head morphogenesis of mouse embryos by activating the Lim1-Ldb1 complex. Nishioka, N., Nagano, S., Nakayama, R., Kiyonari, H., Ijiri, T., Taniguchi, K., Shawlot, W., Hayashizaki, Y., Westphal, H., Behringer, R.R., Matsuda, Y., Sakoda, S., Kondoh, H., Sasaki, H. Development (2005) [Pubmed]
  9. Identification of the LMO4 gene encoding an interaction partner of the LIM-binding protein LDB1/NLI1: a candidate for displacement by LMO proteins in T cell acute leukaemia. Grutz, G., Forster, A., Rabbitts, T.H. Oncogene (1998) [Pubmed]
  10. Expression of LIM-domain binding protein (ldb) genes during zebrafish embryogenesis. Toyama, R., Kobayashi, M., Tomita, T., Dawid, I.B. Mech. Dev. (1998) [Pubmed]
  11. Functional ablation of the mouse Ldb1 gene results in severe patterning defects during gastrulation. Mukhopadhyay, M., Teufel, A., Yamashita, T., Agulnick, A.D., Chen, L., Downs, K.M., Schindler, A., Grinberg, A., Huang, S.P., Dorward, D., Westphal, H. Development (2003) [Pubmed]
  12. Genomic structure and chromosomal localization of the mouse LIM domain-binding protein 1 gene, Ldb1. Yamashita, T., Agulnick, A.D., Copeland, N.G., Gilbert, D.J., Jenkins, N.A., Westphal, H. Genomics (1998) [Pubmed]
  13. Conserved regulation of mesenchymal gene expression by Fgf-8 in face and limb development. Tucker, A.S., Al Khamis, A., Ferguson, C.A., Bach, I., Rosenfeld, M.G., Sharpe, P.T. Development (1999) [Pubmed]
  14. Identification of a protein that interacts with the golli-myelin basic protein and with nuclear LIM interactor in the nervous system. Fernandes, A.O., Campagnoni, C.W., Kampf, K., Feng, J.M., Handley, V.W., Schonmann, V., Bongarzone, E.R., Reyes, S., Campagnoni, A.T. J. Neurosci. Res. (2004) [Pubmed]
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