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Gene Review

EPB41L3  -  erythrocyte membrane protein band 4.1-like 3

Homo sapiens

Synonyms: 4.1B, Band 4.1-like protein 3, DAL-1, DAL1, Differentially expressed in adenocarcinoma of the lung protein 1, ...
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Disease relevance of EPB41L3


High impact information on EPB41L3

  • Analogous to merlin, we show that DAL-1 loss is an early event in meningioma tumorigenesis, suggesting that these two protein 4.1 family members are critical growth regulators in the pathogenesis of meningiomas [1].
  • Loss of DAL-1, a protein 4.1-related tumor suppressor, is an important early event in the pathogenesis of meningiomas [1].
  • Previous studies from our laboratory have shown that protein 4.1B growth suppression in meningioma is associated with the activation of the c-Jun-NH(2)-kinase (JNK) pathway and requires localization of a small unique region (U2 domain) of protein 4.1B to the plasma membrane [5].
  • Protein 4.1B/differentially expressed in adenocarcinoma of the lung-1 functions as a growth suppressor in meningioma cells by activating Rac1-dependent c-Jun-NH(2)-kinase signaling [5].
  • Here, we report that TSLC1 directly associates with DAL-1, a gene product of another lung tumor suppressor belonging to the protein 4.1 family [6].

Chemical compound and disease context of EPB41L3


Biological context of EPB41L3


Anatomical context of EPB41L3

  • DAL-1/4.1B is normally expressed at high levels in the brain, with lower levels in the kidney, intestine, and testis [9].
  • We propose that 4.1B anchors these axonal proteins to the actin-based cytoskeleton in these two regions [10].
  • Immunocytochemical staining with a polyclonal anti-DAL-1 antibody localized the protein to the plasma membrane, particularly at cell-cell contact points, a pattern reminiscent of other members of the protein 4.1 superfamily including ezrin and NF2 [11].
  • In addition, expression of DAL-1 increased attachment of these cells to a variety of extracellular matrices [12].
  • Human DAL-1 was also expressed in matured epithelial cells in human colons, with a definite expression gradient along the crypt axis [13].

Associations of EPB41L3 with chemical compounds

  • Moreover, similar to wild-type DAL-1, the stable expression of the DAL-1 F359Y mutant significantly reduced cell proliferation in independently isolated IOMM-Lee clones, as assessed by thymidine incorporation [14].
  • Expression and allelic and methylation status of DAL-1 was examined by reverse transcription-PCR, microsatellite analysis, and bisulfite sequencing or bisulfite single-strand conformational polymorphism, respectively [15].
  • Similar to the Protein 4.1B and merlin tumor suppressors, Protein 4.1R membrane localization increased significantly under conditions of growth arrest in vitro [16].
  • Moreover, the immunolocalization of protein 4.1B was almost the same as that of NBC-1, indicating a possible function as a regulator of ion balance, such as Na(+) and HCO(3)(-) reabsorption [17].

Other interactions of EPB41L3

  • Our results suggest that methylation of TSLC1 and/or DAL-1, leading to loss of their expression, is an important event in the pathogenesis of NSCLC [7].
  • However, little is known about the other two genes in this cascade, DAL-1 and MPP3 [7].
  • In this study, we assessed the impact of DAL-1/4.1B binding on the activity of another family member, PRMT5, both in vitro and in cells [18].
  • This was due to a decrease in the ability of 4.1G and 4.1B SAB domain to interact with actin but not with spectrin [19].
  • Comparative transcript abundance was analysed in heart and brain. betaIISigma2-spectrin was the most abundant transcript in heart with levels 5 fold greater than 4.1G or 4.1N and at least 9 fold greater than 4.1B [20].

Analytical, diagnostic and therapeutic context of EPB41L3


  1. Loss of DAL-1, a protein 4.1-related tumor suppressor, is an important early event in the pathogenesis of meningiomas. Gutmann, D.H., Donahoe, J., Perry, A., Lemke, N., Gorse, K., Kittiniyom, K., Rempel, S.A., Gutierrez, J.A., Newsham, I.F. Hum. Mol. Genet. (2000) [Pubmed]
  2. DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo. Singh, V., Miranda, T.B., Jiang, W., Frankel, A., Roemer, M.E., Robb, V.A., Gutmann, D.H., Herschman, H.R., Clarke, S., Newsham, I.F. Oncogene (2004) [Pubmed]
  3. The protein 4.1 tumor suppressor, DAL-1, impairs cell motility, but regulates proliferation in a cell-type-specific fashion. Gutmann, D.H., Hirbe, A.C., Huang , Z.Y., Haipek, C.A. Neurobiol. Dis. (2001) [Pubmed]
  4. Alterations of protein 4.1 family members in ependymomas: a study of 84 cases. Rajaram, V., Gutmann, D.H., Prasad, S.K., Mansur, D.B., Perry, A. Mod. Pathol. (2005) [Pubmed]
  5. Protein 4.1B/differentially expressed in adenocarcinoma of the lung-1 functions as a growth suppressor in meningioma cells by activating Rac1-dependent c-Jun-NH(2)-kinase signaling. Gerber, M.A., Bahr, S.M., Gutmann, D.H. Cancer Res. (2006) [Pubmed]
  6. Direct association of TSLC1 and DAL-1, two distinct tumor suppressor proteins in lung cancer. Yageta, M., Kuramochi, M., Masuda, M., Fukami, T., Fukuhara, H., Maruyama, T., Shibuya, M., Murakami, Y. Cancer Res. (2002) [Pubmed]
  7. Expression and methylation pattern of TSLC1 cascade genes in lung carcinomas. Heller, G., Fong, K.M., Girard, L., Seidl, S., End-Pfützenreuter, A., Lang, G., Gazdar, A.F., Minna, J.D., Zielinski, C.C., Zöchbauer-Müller, S. Oncogene (2006) [Pubmed]
  8. Allele-specific loss of heterozygosity at the DAL-1/4.1B (EPB41L3) tumor-suppressor gene locus in the absence of mutation. Kittiniyom, K., Mastronardi, M., Roemer, M., Wells, W.A., Greenberg, E.R., Titus-Ernstoff, L., Newsham, I.F. Genes Chromosomes Cancer (2004) [Pubmed]
  9. Mutational analysis of the DAL-1/4.1B tumour-suppressor gene locus in meningiomas. Martinez-Glez, V., Bello, M.J., Franco-Hernandez, C., De Campos, J.M., Isla, A., Vaquero, J., Rey, J.A. Int. J. Mol. Med. (2005) [Pubmed]
  10. Protein 4.1B associates with both Caspr/paranodin and Caspr2 at paranodes and juxtaparanodes of myelinated fibres. Denisenko-Nehrbass, N., Oguievetskaia, K., Goutebroze, L., Galvez, T., Yamakawa, H., Ohara, O., Carnaud, M., Girault, J.A. Eur. J. Neurosci. (2003) [Pubmed]
  11. A novel member of the NF2/ERM/4.1 superfamily with growth suppressing properties in lung cancer. Tran, Y.K., Bögler, O., Gorse, K.M., Wieland, I., Green, M.R., Newsham, I.F. Cancer Res. (1999) [Pubmed]
  12. Suppression of growth and increased cellular attachment after expression of DAL-1 in MCF-7 breast cancer cells. Charboneau, A.L., Singh, V., Yu, T., Newsham, I.F. Int. J. Cancer (2002) [Pubmed]
  13. Immunolocalization of protein 4.1B/DAL-1 during neoplastic transformation of mouse and human intestinal epithelium. Ohno, N., Terada, N., Murata, S., Yamakawa, H., Newsham, I.F., Katoh, R., Ohara, O., Ohno, S. Histochem. Cell Biol. (2004) [Pubmed]
  14. Disruption of 14-3-3 binding does not impair Protein 4.1B growth suppression. Robb, V.A., Li, W., Gutmann, D.H. Oncogene (2004) [Pubmed]
  15. Promoter methylation of DAL-1/4.1B predicts poor prognosis in non-small cell lung cancer. Kikuchi, S., Yamada, D., Fukami, T., Masuda, M., Sakurai-Yageta, M., Williams, Y.N., Maruyama, T., Asamura, H., Matsuno, Y., Onizuka, M., Murakami, Y. Clin. Cancer Res. (2005) [Pubmed]
  16. Identification of a third Protein 4.1 tumor suppressor, Protein 4.1R, in meningioma pathogenesis. Robb, V.A., Li, W., Gascard, P., Perry, A., Mohandas, N., Gutmann, D.H. Neurobiol. Dis. (2003) [Pubmed]
  17. Immunoelectron microscopic localization of protein 4.1B in proximal S1 and S2 tubules of rodent kidneys. Terada, N., Ohno, N., Yamakawa, H., Seki, G., Fujii, Y., Baba, T., Ohara, O., Ohno, S. Medical electron microscopy : official journal of the Clinical Electron Microscopy Society of Japan. (2004) [Pubmed]
  18. The tumor suppressor DAL-1/4.1B modulates protein arginine N-methyltransferase 5 activity in a substrate-specific manner. Jiang, W., Roemer, M.E., Newsham, I.F. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  19. Functional characterization of spectrin-actin-binding domains in 4.1 family of proteins. Gimm, J.A., An, X., Nunomura, W., Mohandas, N. Biochemistry (2002) [Pubmed]
  20. Expression of human membrane skeleton protein genes for protein 4.1 and betaIISigma2-spectrin assayed by real-time RT-PCR. Taylor-Harris, P.M., Felkin, L.E., Birks, E.J., Franklin, R.C., Yacoub, M.H., Baines, A.J., Barton, P.J., Pinder, J.C. Cell. Mol. Biol. Lett. (2005) [Pubmed]
  21. Clear cell ependymoma: a clinicopathologic and radiographic analysis of 10 patients. Fouladi, M., Helton, K., Dalton, J., Gilger, E., Gajjar, A., Merchant, T., Kun, L., Newsham, I., Burger, P., Fuller, C. Cancer (2003) [Pubmed]
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