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Dmtn  -  dematin actin binding protein

Mus musculus

Synonyms: AI325486, Dematin, Dematin actin-binding protein, Epb4.9, Epb49, ...
 
 
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Disease relevance of Epb4.9

 

High impact information on Epb4.9

  • In vitro membrane stability measurements indicated significantly greater membrane fragmentation of the dematin headpiece null erythrocytes [2].
  • By using homologous recombination in mouse embryonic stem cells, the headpiece domain of dematin was deleted to evaluate its function in vivo [2].
  • Dematin is localized to the spectrin-actin junctions, and its actin-bundling activity is regulated by phosphorylation of cAMP-dependent protein kinase [2].
  • The carboxyl terminus of dematin is homologous to the "headpiece" domain of villin, an actin-bundling protein of the microvillus cytoskeleton [2].
  • Together, these results reveal an essential role of dematin and adducin in the maintenance of erythrocyte shape and membrane stability, and they suggest that the dematin-membrane interaction could link the junctional complex to the plasma membrane in erythroid cells [3].
 

Biological context of Epb4.9

 

Anatomical context of Epb4.9

  • Together, these results provide evidence for the physiological significance of dematin and demonstrate a role for the headpiece domain in the maintenance of structural integrity and mechanical properties of erythrocytes in vivo [2].
  • Transcripts of dematin are widely distributed including human brain, heart, lung, skeletal muscle, and kidney [5].
  • Dematin is a cytoskeletal protein that bundles actin filaments in a phosphorylation-dependent manner [1].
  • Conversely, the heterologous expression of dominant negative mutants of dematin perturbed normal cell morphology of NIH 3T3 fibroblasts [1].
 

Associations of Epb4.9 with chemical compounds

 

Other interactions of Epb4.9

 

Analytical, diagnostic and therapeutic context of Epb4.9

References

  1. Loss of heterozygosity on 8p in prostate cancer implicates a role for dematin in tumor progression. Lutchman, M., Pack, S., Kim, A.C., Azim, A., Emmert-Buck, M., van Huffel, C., Zhuang, Z., Chishti, A.H. Cancer Genet. Cytogenet. (1999) [Pubmed]
  2. Headpiece domain of dematin is required for the stability of the erythrocyte membrane. Khanna, R., Chang, S.H., Andrabi, S., Azam, M., Kim, A., Rivera, A., Brugnara, C., Low, P.S., Liu, S.C., Chishti, A.H. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. Combined Deletion of Mouse Dematin-Headpiece and beta-Adducin Exerts a Novel Effect on the Spectrin-Actin Junctions Leading to Erythrocyte Fragility and Hemolytic Anemia. Chen, H., Khan, A.A., Liu, F., Gilligan, D.M., Peters, L.L., Messick, J., Haschek-Hock, W.M., Li, X., Ostafin, A.E., Chishti, A.H. J. Biol. Chem. (2007) [Pubmed]
  4. The gene encoding the erythrocyte membrane skeleton protein dematin (Epb4.9) maps to mouse chromosome 14. Peters, L.L., Eicher, E.M., Azim, A.C., Chishti, A.H. Genomics (1995) [Pubmed]
  5. Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2 and modulates mitogen-activated protein kinase pathways. Lutchman, M., Kim, A.C., Cheng, L., Whitehead, I.P., Oh, S.S., Hanspal, M., Boukharov, A.A., Hanada, T., Chishti, A.H. Eur. J. Biochem. (2002) [Pubmed]
  6. A 52 kD cytoskeletal protein from retinal rod photoreceptors is related to erythrocyte dematin. Roof, D., Hayes, A., Hardenbergh, G., Adamian, M. Invest. Ophthalmol. Vis. Sci. (1991) [Pubmed]
 
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