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Apc  -  APC-like

Drosophila melanogaster

Synonyms: APC, APC1, Apc1, CG1451, D-APC, ...
 
 
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Disease relevance of Apc

  • Mutations in the adenomatous polyposis coli gene (which encodes a protein called APC) are associated with the formation of intestinal polyps and colon cancers [1].
  • Inactivation of the Adenomatous Polyposis Coli (APC) tumor suppressor triggers the development of most colorectal carcinomas [2].
  • These results indicate that Drosophila APC functions in cellular adhesion; these results could have implications for colorectal adenoma formation and tumour progression in humans [3].
  • Retinal degeneration in the D-APC mutant results from apoptotic cell death, which accompanies a defect in neuronal differentiation [4].
 

High impact information on Apc

 

Biological context of Apc

 

Anatomical context of Apc

 

Physical interactions of Apc

  • This is achieved by Shot association with the cytoplasmic faces of the basal hemiadherens junction and with the EB1/APC1 complex [12].
 

Other interactions of Apc

  • Drosophila Apc1 and Apc2 regulate Wingless transduction throughout development [2].
  • This region interacts with C-cadherin and with the APC tumor suppressor protein, but not with alpha-catenin, that requires the amino-terminal region of beta-catenin to bind to the complex [13].
  • In addition, we show that the retinal apoptosis previously reported in apc1 mutants occurs at the same time as the peripheral ommatidial cell death and also depends on head involution defective, grim and reaper [14].
  • Shortstop recruits EB1/APC1 and promotes microtubule assembly at the muscle-tendon junction [12].
  • In tendon cells with reduced Shot activity, EB1/APC1 dissociate from the muscle-tendon junction, and the microtubule array elongates [12].
 

Analytical, diagnostic and therapeutic context of Apc

References

  1. A Drosophila homolog of the tumor suppressor gene adenomatous polyposis coli down-regulates beta-catenin but its zygotic expression is not essential for the regulation of Armadillo. Hayashi, S., Rubinfeld, B., Souza, B., Polakis, P., Wieschaus, E., Levine, A.J. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  2. Drosophila Apc1 and Apc2 regulate Wingless transduction throughout development. Ahmed, Y., Nouri, A., Wieschaus, E. Development (2002) [Pubmed]
  3. A Drosophila APC tumour suppressor homologue functions in cellular adhesion. Hamada, F., Bienz, M. Nat. Cell Biol. (2002) [Pubmed]
  4. Regulation of armadillo by a Drosophila APC inhibits neuronal apoptosis during retinal development. Ahmed, Y., Hayashi, S., Levine, A., Wieschaus, E. Cell (1998) [Pubmed]
  5. Independent regulation of synaptic size and activity by the anaphase-promoting complex. van Roessel, P., Elliott, D.A., Robinson, I.M., Prokop, A., Brand, A.H. Cell (2004) [Pubmed]
  6. The APC tumour suppressor has a nuclear export function. Rosin-Arbesfeld, R., Townsley, F., Bienz, M. Nature (2000) [Pubmed]
  7. Binding of APC to the human homolog of the Drosophila discs large tumor suppressor protein. Matsumine, A., Ogai, A., Senda, T., Okumura, N., Satoh, K., Baeg, G.H., Kawahara, T., Kobayashi, S., Okada, M., Toyoshima, K., Akiyama, T. Science (1996) [Pubmed]
  8. The dominant mutation Glazed is a gain-of-function allele of wingless that, similar to loss of APC, interferes with normal eye development. Brunner, E., Brunner, D., Fu, W., Hafen, E., Basler, K. Dev. Biol. (1999) [Pubmed]
  9. Identification and characterization of E-APC, a novel Drosophila homologue of the tumour suppressor APC. Hamada, F., Murata, Y., Nishida, A., Fujita, F., Tomoyasu, Y., Nakamura, M., Toyoshima, K., Tabata, T., Ueno, N., Akiyama, T. Genes Cells (1999) [Pubmed]
  10. Actin-dependent membrane association of a Drosophila epithelial APC protein and its effect on junctional Armadillo. Townsley, F.M., Bienz, M. Curr. Biol. (2000) [Pubmed]
  11. Drosophila APC2 and APC1 have overlapping roles in the larval brain despite their distinct intracellular localizations. Akong, K., McCartney, B.M., Peifer, M. Dev. Biol. (2002) [Pubmed]
  12. Shortstop recruits EB1/APC1 and promotes microtubule assembly at the muscle-tendon junction. Subramanian, A., Prokop, A., Yamamoto, M., Sugimura, K., Uemura, T., Betschinger, J., Knoblich, J.A., Volk, T. Curr. Biol. (2003) [Pubmed]
  13. Embryonic axis induction by the armadillo repeat domain of beta-catenin: evidence for intracellular signaling. Funayama, N., Fagotto, F., McCrea, P., Gumbiner, B.M. J. Cell Biol. (1995) [Pubmed]
  14. Wingless eliminates ommatidia from the edge of the developing eye through activation of apoptosis. Lin, H.V., Rogulja, A., Cadigan, K.M. Development (2004) [Pubmed]
  15. Activation of B cells using Schneider 2 cells expressing CD40 ligand for the enhancement of antigen presentation in vitro. Yoon, S.H., Cho, H.I., Kim, T.G. Exp. Mol. Med. (2005) [Pubmed]
 
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