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Gene Review

LMO4  -  LIM domain only 4

Homo sapiens

Synonyms: Breast tumor autoantigen, LIM domain only protein 4, LIM domain transcription factor LMO4, LMO-4
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Disease relevance of LMO4


Psychiatry related information on LMO4


High impact information on LMO4

  • Down-regulation of LMO4 expression reduced proliferation of human breast cancer cells and increased differentiation of mouse mammary epithelial cells [3].
  • Together, these findings suggest that deregulation of LMO4 in breast epithelium contributes directly to breast neoplasia by altering the rate of cellular proliferation and promoting cell invasion [3].
  • The zinc finger protein LMO4 is overexpressed in a high proportion of breast carcinomas [3].
  • Conversely, overexpression of LMO4 in noninvasive, immortalized human MCF10A cells promoted cell motility and invasion [3].
  • To investigate cellular processes controlled by LMO4 and those that may be deregulated during oncogenesis, we used RNA interference [3].

Biological context of LMO4


Anatomical context of LMO4

  • Expression of the LMO4 gene is developmentally regulated in the mammary gland and is up-regulated in primary breast cancers [1].
  • Sequestration of Ldb1 by LMO2 in T-cells may prevent it binding other key partners, such as LMO4 [9].
  • Mutation analysis of the coding and 3' untranslated regions of the LMO4 gene was performed on 82 primary breast and 22 tumor cell lines [2].
  • Overexpression of HEN1 in hippocampal precursor cells resulted in neurite extension, which could be prevented by LMO4 [7].
  • Consistent with this, silencing LMO4 expression in stable cell lines expressing the small interfering RNA of LMO4 decreased Stat3 activity [8].

Associations of LMO4 with chemical compounds


Other interactions of LMO4

  • Using LMO4 in a yeast two-hybrid screen, we have identified the cofactor CtIP as an LMO4-binding protein [1].
  • LMO4 belongs to the LIM-only (LMO) group of transcriptional regulators that appear to function as molecular adaptors for protein-protein interactions [1].
  • Consistent with this notion, LMO4 overexpression repressed ERalpha transactivation functions in an HDAC-dependent manner [4].
  • Immunocytochemical analysis revealed a high level of LMO4 expression in the entorhinal cortex (EC) and in the CA1 hippocampal region of the control brains and a consistent decrease in the AD brains, correlated with the amount of neurofibrillary tangles (NFT) degenerating neurones and the severity of senile plaques deposition [6].
  • We next applied the biotinylation tag to Ldb-1, a known partner of GATA-1, and characterized a number of novel interaction partners that are essential in erythroid development, in particular, Eto-2, Lmo4, and CdK9 [10].

Analytical, diagnostic and therapeutic context of LMO4


  1. The LIM domain protein LMO4 interacts with the cofactor CtIP and the tumor suppressor BRCA1 and inhibits BRCA1 activity. Sum, E.Y., Peng, B., Yu, X., Chen, J., Byrne, J., Lindeman, G.J., Visvader, J.E. J. Biol. Chem. (2002) [Pubmed]
  2. Mutational analysis of the LMO4 gene, encoding a BRCA1-interacting protein, in breast carcinomas. Sutherland, K.D., Visvader, J.E., Choong, D.Y., Sum, E.Y., Lindeman, G.J., Campbell, I.G. Int. J. Cancer (2003) [Pubmed]
  3. Overexpression of LMO4 induces mammary hyperplasia, promotes cell invasion, and is a predictor of poor outcome in breast cancer. Sum, E.Y., Segara, D., Duscio, B., Bath, M.L., Field, A.S., Sutherland, R.L., Lindeman, G.J., Visvader, J.E. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  4. Negative regulation of estrogen receptor alpha transactivation functions by LIM domain only 4 protein. Singh, R.R., Barnes, C.J., Talukder, A.H., Fuqua, S.A., Kumar, R. Cancer Res. (2005) [Pubmed]
  5. Transcription regulator LMO4 interferes with neuritogenesis in human SH-SY5Y neuroblastoma cells. Vu, D., Marin, P., Walzer, C., Cathieni, M.M., Bianchi, E.N., Saïdji, F., Leuba, G., Bouras, C., Savioz, A. Brain Res. Mol. Brain Res. (2003) [Pubmed]
  6. Differential expression of LMO4 protein in Alzheimer's disease. Leuba, G., Vernay, A., Vu, D., Walzer, C., Belloir, B., Kraftsik, R., Bouras, C., Savioz, A. Neuropathol. Appl. Neurobiol. (2004) [Pubmed]
  7. The LIM-only protein LMO4 modulates the transcriptional activity of HEN1. Manetopoulos, C., Hansson, A., Karlsson, J., Jönsson, J.I., Axelson, H. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  8. Modulation of the interleukin-6 receptor subunit glycoprotein 130 complex and its signaling by LMO4 interaction. Novotny-Diermayr, V., Lin, B., Gu, L., Cao, X. J. Biol. Chem. (2005) [Pubmed]
  9. Identification of the Key LMO2-binding Determinants on Ldb1. Ryan, D.P., Sunde, M., Kwan, A.H., Marianayagam, N.J., Nancarrow, A.L., Vanden Hoven, R.N., Thompson, L.S., Baca, M., Mackay, J.P., Visvader, J.E., Matthews, J.M. J. Mol. Biol. (2006) [Pubmed]
  10. Isolation and characterization of hematopoietic transcription factor complexes by in vivo biotinylation tagging and mass spectrometry. Grosveld, F., Rodriguez, P., Meier, N., Krpic, S., Pourfarzad, F., Papadopoulos, P., Kolodziej, K., Patrinos, G.P., Hostert, A., Strouboulis, J. Ann. N. Y. Acad. Sci. (2005) [Pubmed]
  11. Characterization of the Lmo4 gene encoding a LIM-only protein: genomic organization and comparative chromosomal mapping. Tse, E., Grutz, G., Garner, A.A., Ramsey, Y., Carter, N.P., Copeland, N., Gilbert, D.J., Jenkins, N.A., Agulnick, A., Forster, A., Rabbitts, T.H. Mamm. Genome (1999) [Pubmed]
  12. Identification and characterization of LMO4, an LMO gene with a novel pattern of expression during embryogenesis. Kenny, D.A., Jurata, L.W., Saga, Y., Gill, G.N. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
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