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Gene Review

LDB1  -  LIM domain binding 1

Homo sapiens

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

  • These data suggest that the LMO4-LDB1 complexes may be involved in carcinoma progression possibly through dedifferentiation of squamous carcinoma cells of the oral cavity [1].
  • Confirmation of CLIM2/LMX1B interaction by yeast two-hybrid screening and analysis of its involvement in nail-patella syndrome [2].
  • Transfection assay to the pituitary tumor derived LbetaT2 cells, and the Chinese hamster ovary cells demonstrated that CLIM2 acts as a corepressor of the porcine Lhx2 function [3].
  • We examined 55 pancreatic adenocarcinoma specimens for TOP2A immunolabeling and identified TOP2A protein expression in all specimens with a nuclear labeling index (NLI; positive nuclei/total nuclei x 100) of 5% to 80% [4].
  • METHODS: We classified 330 patients with a first-ever cerebral infarction in the carotid territory into LI and non-LI (NLI) groups [5].

Psychiatry related information on LDB1

  • With each additional processing demand, response times increased disproportionately for the LI group relative to the NLI group [6].

High impact information on LDB1

  • In addition, NLI was shown to form high affinity homodimers through the amino-terminal 200 amino acids, but dimerization of NLI was not required for association with the LIM homeodomain protein Lmxl [7].
  • The ubiquitous nuclear adaptor protein LIM-domain-binding protein 1 (Ldb1) was originally identified as a cofactor for LIM-homeodomain and LIM-only (LMO) proteins that have fundamental roles in development [8].
  • Moreover, Isl1 could mediate the recruitment of the cofactor CLIM2 resulting in a further transcriptional enhancement of the HNF1alpha promoter activity [9].
  • Although individual transcription factors initiating progression remain unknown, LIM-only protein (LMO) and LIM-domain binding protein (LDB) negatively regulate breast carcinoma cell differentiation [1].
  • The tyrosine missense mutation inhibits the ability of LHX3 to induce transcription from selected target genes but does not prevent DNA binding and interaction with partner proteins such as NLI and Pit-1 [10].

Biological context of LDB1

  • Therefore, the LMO1-LDB1 interaction is likely to be involved in tumorigenesis after LMO1 is ectopically expressed following chromosomal translocation in T cells prior to development of acute leukaemias [11].
  • Genomic structure, alternative transcripts and chromosome location of the human LIM domain binding protein 1 gene LDB1 [12].
  • Among those molecules, cofactor Ldb1, interacting with LIM/homeobox family transcription factor, defines a tetrameric protein complex in controlling downstream genes of transcriptional regulation [13].
  • Moreover, by genotyping a polymorphic dinucleotide repeat close to the CLIM2 gene in affected members of a large Dutch NPS family with high incidence of nephropathy, we were unable to find a correlation between the presence of a specific allele and the expression of nephropathy [2].
  • Interestingly, CLIM2 alone apparently repressed the high level of alphaGSU gene expression in LbetaT2 cells [3].

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 [3].

Other interactions of LDB1

  • By protein interaction screening using a radioactive LMO2 protein probe we have isolated a LIM domain binding protein [12].
  • In this review, the authors describe the progressive discoveries of NLI/Ldb/CLIM, LMO and RLIM, and discuss how the field was very recently updated by the finding that LIM-hd transcriptional activity is controlled by regulated degradation of cofactors and LIM-hd themselves [14].

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 [3].
  • Crystallization of FLINC4, an intramolecular LMO4-ldb1 complex [15].


  1. The LIM-only protein, LMO4, and the LIM domain-binding protein, LDB1, expression in squamous cell carcinomas of the oral cavity. Mizunuma, H., Miyazawa, J., Sanada, K., Imai, K. Br. J. Cancer (2003) [Pubmed]
  2. Confirmation of CLIM2/LMX1B interaction by yeast two-hybrid screening and analysis of its involvement in nail-patella syndrome. Marini, M., Bongers, E.M., Cusano, R., Di Duca, M., Seri, M., Knoers, N.V., Ravazzolo, R. Int. J. Mol. Med. (2003) [Pubmed]
  3. 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]
  4. A subset of pancreatic adenocarcinomas demonstrates coamplification of topoisomerase IIalpha and HER2/neu: use of immunolabeling and multicolor FISH for potential patient screening andtreatment. Hansel, D.E., Ashfaq, R., Rahman, A., Wanzer, D., Yeo, C.J., Wilentz, R.E., Maitra, A. Am. J. Clin. Pathol. (2005) [Pubmed]
  5. Does a relationship exist between carotid stenosis and lacunar infarction? Tejada, J., Díez-Tejedor, E., Hernández-Echebarría, L., Balboa, O. Stroke (2003) [Pubmed]
  6. Speed of information processing in children referred for learning problems: performance on a visual filtering test. Weiler, M.D., Harris, N.S., Marcus, D.J., Bellinger, D., Kosslyn, S.M., Waber, D.P. Journal of learning disabilities. (2000) [Pubmed]
  7. Functional analysis of the nuclear LIM domain interactor NLI. Jurata, L.W., Gill, G.N. Mol. Cell. Biol. (1997) [Pubmed]
  8. LIM-domain-binding protein 1: a multifunctional cofactor that interacts with diverse proteins. Matthews, J.M., Visvader, J.E. EMBO Rep. (2003) [Pubmed]
  9. Hepatocyte Nuclear Factor 4 Alpha Ligand Binding and F Domains Mediate Interaction and Transcriptional Synergy with the Pancreatic Islet LIM HD Transcription Factor Isl1. Eeckhoute, J., Briche, I., Kurowska, M., Formstecher, P., Laine, B. J. Mol. Biol. (2006) [Pubmed]
  10. LHX3 transcription factor mutations associated with combined pituitary hormone deficiency impair the activation of pituitary target genes. Sloop, K.W., Parker, G.E., Hanna, K.R., Wright, H.A., Rhodes, S.J. Gene (2001) [Pubmed]
  11. The LMO1 AND LDB1 proteins interact in human T cell acute leukaemia with the chromosomal translocation t(11;14)(p15;q11). Valge-Archer, V., Forster, A., Rabbitts, T.H. Oncogene (1998) [Pubmed]
  12. Genomic structure, alternative transcripts and chromosome location of the human LIM domain binding protein 1 gene LDB1. Drechsler, M., Schumacher, V., Friedrich, S., Wildhardt, G., Giesler, S., Schroth, A., Bodem, J., Royer-Pokora, B. Cytogenet. Cell Genet. (1999) [Pubmed]
  13. Structure and functional characterization of single-strand DNA binding protein SSDP1: carboxyl-terminal of SSDP1 has transcription activity. Wu, L. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  14. A short history of LIM domains (1993-2002): from protein interaction to degradation. Rétaux, S., Bachy, I. Mol. Neurobiol. (2002) [Pubmed]
  15. Crystallization of FLINC4, an intramolecular LMO4-ldb1 complex. Deane, J.E., Maher, M.J., Langley, D.B., Graham, S.C., Visvader, J.E., Guss, J.M., Matthews, J.M. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]
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