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Gene Review

ARFGEF2  -  ADP-ribosylation factor guanine nucleotide...

Homo sapiens

Synonyms: ADP-ribosylation factor guanine nucleotide-exchange factor 2, ARFGEP2, BIG2, Brefeldin A-inhibited GEP 2, Brefeldin A-inhibited guanine nucleotide-exchange protein 2, ...
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Disease relevance of ARFGEF2

  • Finally, transfection of a dominant-negative construct of ARFGEF2 in SHSY5Y neuroblastoma cells partially blocked FLNA transport from the Golgi apparatus to the cell membrane [1].
  • These phage Ig-like domains fall into three distinct sequence families, which are similar to the classic immunoglobulin domain (I-Set), the fibronectin type 3 repeat (FN3), and the bacterial Ig-like domain (Big2) [2].

High impact information on ARFGEF2

  • Here we show that an autosomal recessive condition characterized by microcephaly and periventricular heterotopia maps to chromosome 20 and is caused by mutations in the gene ADP-ribosylation factor guanine nucleotide-exchange factor-2 (ARFGEF2) [3].
  • Inhibition of BIG2 by BFA, or by a dominant negative ARFGEF2 cDNA, decreases cell proliferation in vitro, suggesting a cell-autonomous regulation of neural expansion [3].
  • Mutations in ARFGEF2 implicate vesicle trafficking in neural progenitor proliferation and migration in the human cerebral cortex [3].
  • By northern-blot analysis, we found that mouse Arfgef2 mRNA levels are highest during embryonic periods of ongoing neuronal proliferation and migration, and by in situ hybridization, we found that the mRNA is widely distributed throughout the embryonic central nervous system (CNS) [3].
  • By electron microscopy, Golgi membranes in BIG1-depleted cells were less sharply defined than those in mock or BIG2 siRNA-treated cells, with more vesicle-like structures at the transface [4].

Biological context of ARFGEF2

  • We show here a requirement for BIG1 (but not BIG2) in glycosylation and function of beta1 [4].

Anatomical context of ARFGEF2


Associations of ARFGEF2 with chemical compounds


Regulatory relationships of ARFGEF2

  • The BIG2 overexpression blocked BFA-induced redistribution from membranes of ARF1 and the AP-1 complex but not that of the COPI complex [10].

Other interactions of ARFGEF2


Analytical, diagnostic and therapeutic context of ARFGEF2

  • Furthermore, overlapping BIG2 and FLNA expression was greatest in these same neuroependymal cells of human embryonic brain and was co-expressed in progenitors by Western blot [1].


  1. Overlapping expression of ARFGEF2 and Filamin A in the neuroependymal lining of the lateral ventricles: insights into the cause of periventricular heterotopia. Lu, J., Tiao, G., Folkerth, R., Hecht, J., Walsh, C., Sheen, V. J. Comp. Neurol. (2006) [Pubmed]
  2. Ig-like domains on bacteriophages: a tale of promiscuity and deceit. Fraser, J.S., Yu, Z., Maxwell, K.L., Davidson, A.R. J. Mol. Biol. (2006) [Pubmed]
  3. Mutations in ARFGEF2 implicate vesicle trafficking in neural progenitor proliferation and migration in the human cerebral cortex. Sheen, V.L., Ganesh, V.S., Topcu, M., Sebire, G., Bodell, A., Hill, R.S., Grant, P.E., Shugart, Y.Y., Imitola, J., Khoury, S.J., Guerrini, R., Walsh, C.A. Nat. Genet. (2004) [Pubmed]
  4. BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required for correct glycosylation and function of integrin beta1. Shen, X., Hong, M.S., Moss, J., Vaughan, M. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  5. Interaction of BIG2, a brefeldin A-inhibited guanine nucleotide-exchange protein, with exocyst protein Exo70. Xu, K.F., Shen, X., Li, H., Pacheco-Rodriguez, G., Moss, J., Vaughan, M. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  6. Association of brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2) with recycling endosomes during transferrin uptake. Shen, X., Xu, K.F., Fan, Q., Pacheco-Rodriguez, G., Moss, J., Vaughan, M. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  7. The Brefeldin A-inhibited Guanine Nucleotide-exchange Protein, BIG2, Regulates the Constitutive Release of TNFR1 Exosome-like Vesicles. Islam, A., Shen, X., Hiroi, T., Moss, J., Vaughan, M., Levine, S.J. J. Biol. Chem. (2007) [Pubmed]
  8. AMY-1 (associate of Myc-1) localization to the trans-Golgi network through interacting with BIG2, a guanine-nucleotide exchange factor for ADP-ribosylation factors. Ishizaki, R., Shin, H.W., Iguchi-Ariga, S.M., Ariga, H., Nakayama, K. Genes Cells (2006) [Pubmed]
  9. Dominant-negative mutant of BIG2, an ARF-guanine nucleotide exchange factor, specifically affects membrane trafficking from the trans-Golgi network through inhibiting membrane association of AP-1 and GGA coat proteins. Shinotsuka, C., Waguri, S., Wakasugi, M., Uchiyama, Y., Nakayama, K. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  10. Overexpression of an ADP-ribosylation factor-guanine nucleotide exchange factor, BIG2, uncouples brefeldin A-induced adaptor protein-1 coat dissociation and membrane tubulation. Shinotsuka, C., Yoshida, Y., Kawamoto, K., Takatsu, H., Nakayama, K. J. Biol. Chem. (2002) [Pubmed]
  11. Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2). Li, H., Adamik, R., Pacheco-Rodriguez, G., Moss, J., Vaughan, M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
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