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FANCG  -  Fanconi anemia, complementation group G

Homo sapiens

 
 
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Disease relevance of FANCG

 

High impact information on FANCG

  • We identified the gene as human XRCC9, a gene which has been shown to complement the MMC-sensitive Chinese hamster mutant UV40, and is suspected to be involved in DNA post-replication repair or cell cycle checkpoint control [5].
  • On treatment with DNA interstrand-cross-linking agents, FANCC and FANCG disruption caused increased clastogenic damage, G2/M arrest, and decreased proliferation [4].
  • RESULTS: FANCC and FANCG disruption abrogated FANCD2 monoubiquitination, confirming an impaired Fanconi anemia pathway function [4].
  • We demonstrate that the FA group G (FANCG) protein is found in mitochondria [6].
  • A physical complex of the Fanconi anemia proteins FANCG/XRCC9 and FANCA [7].
 

Chemical compound and disease context of FANCG

 

Biological context of FANCG

 

Anatomical context of FANCG

 

Associations of FANCG with chemical compounds

 

Physical interactions of FANCG

  • A FANCG mutant truncated at the carboxyl-terminus retained the ability to interact with FANCA [21].
  • We found that FANCG was capable of binding to two separate sites in the BRCA2 protein, located either side of the BRC repeats [22].
  • We found that the C terminus of FANCF interacts directly with FANCG and allows the assembly of other FA proteins into a stable complex [23].
  • The FANCG Fanconi anemia protein interacts with CYP2E1: possible role in protection against oxidative DNA damage [24].
  • FANCG was found to interact with XRCC3, and this interaction was disrupted by the FA-G patient derived mutation L71P [25].
 

Regulatory relationships of FANCG

  • However, a high level of activation was found when FANCA was co-expressed with FANCG, indicating strong, direct interaction between these proteins [26].
  • We found that treatment with TNF-alpha induced FANCG protein expression [27].
 

Other interactions of FANCG

  • To further examine complex assembly, the yeast 3-hybrid system was used to investigate the ability of FANCG to act as a molecular bridge in mediating interaction between other FA proteins [21].
  • Direct interaction of the Fanconi anaemia protein FANCG with BRCA2/FANCD1 [22].
  • The interaction between FANCG and FANCF was ablated by a Leu71Pro mutant of FANCG [21].
  • Using immunoblotting, NM3 and UV40 were found not to express the active monoubiquitinated isoform of the FANCD2 protein, although expression of the FANCD-L isoform was restored in the FANCG cDNA transformants, correlating with the correction of mutagen-sensitivity [12].
  • The amino-terminal region of the FANCA protein is required for FANCG binding, FANCC binding, nuclear localization, and functional activity of the complex [28].
 

Analytical, diagnostic and therapeutic context of FANCG

References

  1. Carboxy terminal region of the Fanconi anemia protein, FANCG/XRCC9, is required for functional activity. Kuang, Y., Garcia-Higuera, I., Moran, A., Mondoux, M., Digweed, M., D'Andrea, A.D. Blood (2000) [Pubmed]
  2. Acquired FANCA dysfunction and cytogenetic instability in adult acute myelogenous leukemia. Lensch, M.W., Tischkowitz, M., Christianson, T.A., Reifsteck, C.A., Speckhart, S.A., Jakobs, P.M., O'Dwyer, M.E., Olson, S.B., Le Beau, M.M., Hodgson, S.V., Mathew, C.G., Larson, R.A., Bagby, G.C. Blood (2003) [Pubmed]
  3. The genetics of FANCC and FANCG in familial pancreatic cancer. Rogers, C.D., van der Heijden, M.S., Brune, K., Yeo, C.J., Hruban, R.H., Kern, S.E., Goggins, M. Cancer Biol. Ther. (2004) [Pubmed]
  4. Targeted disruption of FANCC and FANCG in human cancer provides a preclinical model for specific therapeutic options. Gallmeier, E., Calhoun, E.S., Rago, C., Brody, J.R., Cunningham, S.C., Hucl, T., Gorospe, M., Kohli, M., Lengauer, C., Kern, S.E. Gastroenterology (2006) [Pubmed]
  5. The Fanconi anaemia group G gene FANCG is identical with XRCC9. de Winter, J.P., Waisfisz, Q., Rooimans, M.A., van Berkel, C.G., Bosnoyan-Collins, L., Alon, N., Carreau, M., Bender, O., Demuth, I., Schindler, D., Pronk, J.C., Arwert, F., Hoehn, H., Digweed, M., Buchwald, M., Joenje, H. Nat. Genet. (1998) [Pubmed]
  6. Defective mitochondrial peroxiredoxin-3 results in sensitivity to oxidative stress in Fanconi anemia. Mukhopadhyay, S.S., Leung, K.S., Hicks, M.J., Hastings, P.J., Youssoufian, H., Plon, S.E. J. Cell Biol. (2006) [Pubmed]
  7. A physical complex of the Fanconi anemia proteins FANCG/XRCC9 and FANCA. Waisfisz, Q., de Winter, J.P., Kruyt, F.A., de Groot, J., van der Weel, L., Dijkmans, L.M., Zhi, Y., Arwert, F., Scheper, R.J., Youssoufian, H., Hoatlin, M.E., Joenje, H. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  8. Phosphorylation of fanconi anemia (FA) complementation group G protein, FANCG, at serine 7 is important for function of the FA pathway. Qiao, F., Mi, J., Wilson, J.B., Zhi, G., Bucheimer, N.R., Jones, N.J., Kupfer, G.M. J. Biol. Chem. (2004) [Pubmed]
  9. The human XRCC9 gene corrects chromosomal instability and mutagen sensitivities in CHO UV40 cells. Liu, N., Lamerdin, J.E., Tucker, J.D., Zhou, Z.Q., Walter, C.A., Albala, J.S., Busch, D.B., Thompson, L.H. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  10. The fanconi anemia proteins FANCA and FANCG stabilize each other and promote the nuclear accumulation of the Fanconi anemia complex. Garcia-Higuera, I., Kuang, Y., Denham, J., D'Andrea, A.D. Blood (2000) [Pubmed]
  11. Functional analysis of patient-derived mutations in the Fanconi anemia gene, FANCG/XRCC9. Nakanishi, K., Moran, A., Hays, T., Kuang, Y., Fox, E., Garneau, D., de Oca, R.M., Grompe, M., D'Andrea, A.D. Exp. Hematol. (2001) [Pubmed]
  12. The Chinese hamster FANCG/XRCC9 mutant NM3 fails to express the monoubiquitinated form of the FANCD2 protein, is hypersensitive to a range of DNA damaging agents and exhibits a normal level of spontaneous sister chromatid exchange. Wilson, J.B., Johnson, M.A., Stuckert, A.P., Trueman, K.L., May, S., Bryant, P.E., Meyn, R.E., D'Andrea, A.D., Jones, N.J. Carcinogenesis (2001) [Pubmed]
  13. Four human FANCG polymorphic variants show normal biological function in hamster CHO cells. Hinz, J.M., Nham, P.B., Yamada, N.A., Tebbs, R.S., Salazar, E.P., Hinz, A.K., Mohrenweiser, H.W., Jones, I.M., Thompson, L.H. Mutat. Res. (2006) [Pubmed]
  14. Fanconi anemia FANCG protein in mitigating radiation- and enzyme-induced DNA double-strand breaks by homologous recombination in vertebrate cells. Yamamoto, K., Ishiai, M., Matsushita, N., Arakawa, H., Lamerdin, J.E., Buerstedde, J.M., Tanimoto, M., Harada, M., Thompson, L.H., Takata, M. Mol. Cell. Biol. (2003) [Pubmed]
  15. Germ line Fanconi anemia complementation group C mutations and pancreatic cancer. Couch, F.J., Johnson, M.R., Rabe, K., Boardman, L., McWilliams, R., de Andrade, M., Petersen, G. Cancer Res. (2005) [Pubmed]
  16. Resistance to mitomycin C requires direct interaction between the Fanconi anemia proteins FANCA and FANCG in the nucleus through an arginine-rich domain. Kruyt, F.A., Abou-Zahr, F., Mok, H., Youssoufian, H. J. Biol. Chem. (1999) [Pubmed]
  17. Identification of multiple nuclear export sequences in Fanconi anemia group A protein that contribute to CRM1-dependent nuclear export. Ferrer, M., Rodríguez, J.A., Spierings, E.A., de Winter, J.P., Giaccone, G., Kruyt, F.A. Hum. Mol. Genet. (2005) [Pubmed]
  18. FANCG is phosphorylated at serines 383 and 387 during mitosis. Mi, J., Qiao, F., Wilson, J.B., High, A.A., Schroeder, M.J., Stukenberg, P.T., Moss, A., Shabanowitz, J., Hunt, D.F., Jones, N.J., Kupfer, G.M. Mol. Cell. Biol. (2004) [Pubmed]
  19. Oxidative stress/damage induces multimerization and interaction of Fanconi anemia proteins. Park, S.J., Ciccone, S.L., Beck, B.D., Hwang, B., Freie, B., Clapp, D.W., Lee, S.H. J. Biol. Chem. (2004) [Pubmed]
  20. Human alpha spectrin II and the FANCA, FANCC, and FANCG proteins bind to DNA containing psoralen interstrand cross-links. McMahon, L.W., Sangerman, J., Goodman, S.R., Kumaresan, K., Lambert, M.W. Biochemistry (2001) [Pubmed]
  21. Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems. Gordon, S.M., Buchwald, M. Blood (2003) [Pubmed]
  22. Direct interaction of the Fanconi anaemia protein FANCG with BRCA2/FANCD1. Hussain, S., Witt, E., Huber, P.A., Medhurst, A.L., Ashworth, A., Mathew, C.G. Hum. Mol. Genet. (2003) [Pubmed]
  23. The Fanconi anemia gene product FANCF is a flexible adaptor protein. Léveillé, F., Blom, E., Medhurst, A.L., Bier, P., Laghmani, e.l. .H., Johnson, M., Rooimans, M.A., Sobeck, A., Waisfisz, Q., Arwert, F., Patel, K.J., Hoatlin, M.E., Joenje, H., de Winter, J.P. J. Biol. Chem. (2004) [Pubmed]
  24. The FANCG Fanconi anemia protein interacts with CYP2E1: possible role in protection against oxidative DNA damage. Futaki, M., Igarashi, T., Watanabe, S., Kajigaya, S., Tatsuguchi, A., Wang, J., Liu, J.M. Carcinogenesis (2002) [Pubmed]
  25. Tetratricopeptide-motif-mediated interaction of FANCG with recombination proteins XRCC3 and BRCA2. Hussain, S., Wilson, J.B., Blom, E., Thompson, L.H., Sung, P., Gordon, S.M., Kupfer, G.M., Joenje, H., Mathew, C.G., Jones, N.J. DNA Repair (Amst.) (2006) [Pubmed]
  26. Investigation of Fanconi anemia protein interactions by yeast two-hybrid analysis. Huber, P.A., Medhurst, A.L., Youssoufian, H., Mathew, C.G. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  27. Fanconi anemia protein, FANCG, is a phosphoprotein and is upregulated with FANCA after TNF-alpha treatment. Futaki, M., Watanabe, S., Kajigaya, S., Liu, J.M. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  28. Fanconi anemia proteins FANCA, FANCC, and FANCG/XRCC9 interact in a functional nuclear complex. Garcia-Higuera, I., Kuang, Y., Näf, D., Wasik, J., D'Andrea, A.D. Mol. Cell. Biol. (1999) [Pubmed]
  29. Spectrum and significance of variants and mutations in the Fanconi anaemia group G gene in children with sporadic acute myeloid leukaemia. Meyer, S., Barber, L.M., White, D.J., Will, A.M., Birch, J.M., Kohler, J.A., Ersfeld, K., Blom, E., Joenje, H., Eden, T.O., Malcolm Taylor, G. Br. J. Haematol. (2006) [Pubmed]
  30. Molecular characterization of three novel Fanconi anemia mutations in Israeli Arabs. Tamary, H., Dgany, O., Toledano, H., Shalev, Z., Krasnov, T., Shalmon, L., Schechter, T., Bercovich, D., Attias, D., Laor, R., Koren, A., Yaniv, I. Eur. J. Haematol. (2004) [Pubmed]
 
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