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Epb4.1  -  erythrocyte protein band 4.1

Mus musculus

Synonyms: 4.1R, AI415518, Band 4.1, D4Ertd442e, Elp-1, ...
 
 
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Disease relevance of Epb4.1

 

High impact information on Epb4.1

  • To investigate the molecular abnormality in this disorder, we examined the arrangement of the gene encoding protein 4.1, a membrane skeletal protein of human erythrocytes, in an Algerian family with hereditary elliptocytosis and severe hemolytic anemia due to complete deficiency of protein 4 [2].
  • We assigned the gene for erythrocyte protein 4.1 to the short arm (p) of chromosome 1, within a region from band 32 to the terminus (1p32----1pter) [2].
  • Protein 4.1 forms a stable ternary complex with spectrin and actin, thereby strengthening the reticulum and anchoring it directly to the lipid bilayer or to another intrinsic protein, glycophorin [4].
  • A diverse family of protein 4.1R isoforms is encoded by a complex gene on human chromosome 1 [1].
  • Indeed, we show that beta8 integrin interacts directly with the C-terminal domains of several Band 4.1 proteins and colocalizes with them in cultured astrocytes and in the brain [5].
 

Chemical compound and disease context of Epb4.1

 

Biological context of Epb4.1

  • Exon 16 along with sequences carried by exon 17 is necessary and sufficient to induce formation of fodrin-actin-4.1R ternary complexes [7].
  • Four paralogous protein 4.1 genes map to distinct chromosomes in mouse and human [8].
  • Together, these results suggest that synthesis of structurally distinct 4.1R protein isoforms in various cell types is regulated by a novel mechanism requiring coordination between upstream transcription initiation events and downstream alternative splicing events [9].
  • Among the alternative pre-mRNA splicing events that characterize protein 4.1R gene expression, one involving exon 2' plays a critical role in regulating translation initiation and N-terminal protein structure [9].
  • RNA blot analyses revealed that 1A transcripts increase in abundance in late erythroblasts, consistent with the previously demonstrated up-regulation of 80-kDa 4.1R during terminal erythroid differentiation [9].
 

Anatomical context of Epb4.1

 

Associations of Epb4.1 with chemical compounds

  • Distinct distribution of specific members of protein 4.1 gene family in the mouse nephron [10].
  • By analogy with the roles of 4.1R in red blood cells, 4.1N may function to confer stability and plasticity to the neuronal membrane via interactions with multiple binding partners, including the spectrin-actin-based cytoskeleton, integral membrane channels and receptors, and membrane-associated guanylate kinases [12].
  • Enhanced expression of multiple protein tyrosine phosphatases in the regenerating mouse liver: isolation of PTP-RL10, a novel cytoplasmic-type phosphatase with sequence homology to cytoskeletal protein 4.1 [13].
  • Shared epitopes of glycoprotein A and protein 4.1 defined by antibody NaM10-3C10 [14].
 

Physical interactions of Epb4.1

 

Regulatory relationships of Epb4.1

 

Other interactions of Epb4.1

  • Asynchronous regulation of splicing events within protein 4.1 pre-mRNA during erythroid differentiation [17].
  • Molecular and functional characterization of protein 4.1B, a novel member of the protein 4.1 family with high level, focal expression in brain [16].
  • The mouse Ptpro gene was mapped to chromosome 4, closely linked to D4Mit16 and Elp1 (elliptocytosis-1), by using genomic DNAs from a (C57BL/6J x Mus spretus)F1 x Mus spretus backcross [18].
  • A novel neuron-enriched homolog of the erythrocyte membrane cytoskeletal protein 4.1 [12].
  • The N-terminal domain contains several conserved sections (e.g., residues 57-86, 102-164, 219-347, and 375-403), some of which may contribute to binding sites for ankyrin, protein 4.1, or protein 4 [19].
 

Analytical, diagnostic and therapeutic context of Epb4.1

  • The 4.1R knockout mice represent a valuable animal model for exploring 4.1R function in nonerythroid cells and for determining pathophysiological sequelae to 4.1R deficiency [1].
  • Like 4.1R, 4.1N has multiple splice forms as evidenced by PCR and Western analysis [12].
  • Here, we examined 4.1R expression by in situ hybridization analysis and found that 4.1R was selectively expressed in hematopoietic tissues and in specific neuronal populations [6].
  • Molecular cloning and characterization of the protein 4.1O gene, a novel member of the protein 4.1 family with focal expression in ovary [20].

References

  1. Protein 4.1R-deficient mice are viable but have erythroid membrane skeleton abnormalities. Shi, Z.T., Afzal, V., Coller, B., Patel, D., Chasis, J.A., Parra, M., Lee, G., Paszty, C., Stevens, M., Walensky, L., Peters, L.L., Mohandas, N., Rubin, E., Conboy, J.G. J. Clin. Invest. (1999) [Pubmed]
  2. Molecular basis of hereditary elliptocytosis due to protein 4.1 deficiency. Conboy, J., Mohandas, N., Tchernia, G., Kan, Y.W. N. Engl. J. Med. (1986) [Pubmed]
  3. The synthesis and accumulation of membrane protein 4.1 in Friend erythroleukemia cells. Benabdallah, K., Boivin, P., Dhermy, D. Biol. Cell (1991) [Pubmed]
  4. Appearance of new variants of membrane skeletal protein 4.1 during terminal differentiation of avian erythroid and lenticular cells. Granger, B.L., Lazarides, E. Nature (1985) [Pubmed]
  5. An interaction between {alpha}v{beta}8 integrin and Band 4.1B via a highly conserved region of the Band 4.1 C-terminal domain. McCarty, J.H., Cook, A.A., Hynes, R.O. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  6. Neurobehavioral deficits in mice lacking the erythrocyte membrane cytoskeletal protein 4.1. Walensky, L.D., Shi, Z.T., Blackshaw, S., DeVries, A.C., Demas, G.E., Gascard, P., Nelson, R.J., Conboy, J.G., Rubin, E.M., Snyder, S.H., Mohandas, N. Curr. Biol. (1998) [Pubmed]
  7. The prototypical 4.1R-10-kDa domain and the 4.1g-10-kDa paralog mediate fodrin-actin complex formation. Kontrogianni-Konstantopoulos, A., Frye, C.S., Benz, E.J., Huang, S.C. J. Biol. Chem. (2001) [Pubmed]
  8. Four paralogous protein 4.1 genes map to distinct chromosomes in mouse and human. Peters, L.L., Weier, H.U., Walensky, L.D., Snyder, S.H., Parra, M., Mohandas, N., Conboy, J.G. Genomics (1998) [Pubmed]
  9. Alternative 5' exons and differential splicing regulate expression of protein 4.1R isoforms with distinct N-termini. Parra, M.K., Gee, S.L., Koury, M.J., Mohandas, N., Conboy, J.G. Blood (2003) [Pubmed]
  10. Distinct distribution of specific members of protein 4.1 gene family in the mouse nephron. Ramez, M., Blot-Chabaud, M., Cluzeaud, F., Chanan, S., Patterson, M., Walensky, L.D., Marfatia, S., Baines, A.J., Chasis, J.A., Conboy, J.G., Mohandas, N., Gascard, P. Kidney Int. (2003) [Pubmed]
  11. Evolutionarily conserved alternative pre-mRNA splicing regulates structure and function of the spectrin-actin binding domain of erythroid protein 4.1. Winardi, R., Discher, D., Kelley, C., Zon, L., Mays, K., Mohandas, N., Conboy, J.G. Blood (1995) [Pubmed]
  12. A novel neuron-enriched homolog of the erythrocyte membrane cytoskeletal protein 4.1. Walensky, L.D., Blackshaw, S., Liao, D., Watkins, C.C., Weier, H.U., Parra, M., Huganir, R.L., Conboy, J.G., Mohandas, N., Snyder, S.H. J. Neurosci. (1999) [Pubmed]
  13. Enhanced expression of multiple protein tyrosine phosphatases in the regenerating mouse liver: isolation of PTP-RL10, a novel cytoplasmic-type phosphatase with sequence homology to cytoskeletal protein 4.1. Higashitsuji, H., Arii, S., Furutani, M., Imamura, M., Kaneko, Y., Takenawa, J., Nakayama, H., Fujita, J. Oncogene (1995) [Pubmed]
  14. Shared epitopes of glycoprotein A and protein 4.1 defined by antibody NaM10-3C10. Rasamoelisolo, M., Czerwinski, M., Willem, C., Blanchard, D. Hybridoma (1998) [Pubmed]
  15. Identification of an amelin isoform located in axons. Zimmer, W.E., Zagon, I.S., Casoria, L.A., Goodman, S.R. Brain Res. (1992) [Pubmed]
  16. Molecular and functional characterization of protein 4.1B, a novel member of the protein 4.1 family with high level, focal expression in brain. Parra, M., Gascard, P., Walensky, L.D., Gimm, J.A., Blackshaw, S., Chan, N., Takakuwa, Y., Berger, T., Lee, G., Chasis, J.A., Snyder, S.H., Mohandas, N., Conboy, J.G. J. Biol. Chem. (2000) [Pubmed]
  17. Asynchronous regulation of splicing events within protein 4.1 pre-mRNA during erythroid differentiation. Baklouti, F., Huang, S.C., Tang, T.K., Delaunay, J., Marchesi, V.T., Benz, E.J. Blood (1996) [Pubmed]
  18. Characterization and chromosomal localization of PTPRO, a novel receptor protein tyrosine phosphatase, expressed in hematopoietic stem cells. Avraham, S., London, R., Tulloch, G.A., Ellis, M., Fu, Y., Jiang, S., White, R.A., Painter, C., Steinberger, A.A., Avraham, H. Gene (1997) [Pubmed]
  19. Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1). Lux, S.E., John, K.M., Kopito, R.R., Lodish, H.F. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  20. Molecular cloning and characterization of the protein 4.1O gene, a novel member of the protein 4.1 family with focal expression in ovary. Ni, X., Ji, C., Cao, G., Cheng, H., Guo, L., Gu, S., Ying, K., Zhao, R.C., Mao, Y. J. Hum. Genet. (2003) [Pubmed]
 
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