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Gene Review

GBF1  -  golgi brefeldin A resistant guanine...

Homo sapiens

Synonyms: ARF1GEF, BFA-resistant GEF 1, Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1, KIAA0248
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Disease relevance of GBF1

  • Taken together, our data demonstrate that the activity of the enterovirus 3A protein to inhibit GBF1-dependent COP-I recruitment is unique among the picornaviruses [1].

High impact information on GBF1

  • Hexahistidine-tagged-GBF1 exhibited BFA-resistant guanine nucleotide exchange activity that appears specific towards ARF5 at physiological Mg2+concentration [2].
  • Characterization of cDNAs recovered from the mutant and wild-type parental lines established that transcripts in these cells had identical sequence and, therefore, that GBF1 was naturally BFA resistant [2].
  • Expression cloning from a cDNA library prepared from a mutant CHO cell line with Golgi-specific resistance to Brefeldin A (BFA) identified a novel 206-kD protein with a Sec7 domain termed GBF1 for Golgi BFA resistance factor 1 [2].
  • The mechanism of GBF1 binding to membranes is unknown [3].
  • The drug brefeldin A (BFA), an uncompetitive inhibitor of the exchange reaction that binds to an Arf-GDP-Arf GEF complex, stabilizes GBF1 on Golgi membranes [3].

Biological context of GBF1

  • Mutagenesis analysis indicates that the interaction is not required for targeting GBF1 or p115 to membranes [4].
  • Our findings imply that the continuous recruitment of GBF1 to spatially differentiated membrane domains is required for sustained membrane remodeling that underlies membrane traffic and Golgi biogenesis [5].
  • When the N-terminal residues of the HRV 3A proteins are replaced by those of CVB3 3A, chimeric proteins are produced that have gained the ability to bind GBF1 and, by consequence, to inhibit protein transport [1].
  • Sequencing of genomic DNA for CHO GBF1 and analysis of the human gene established that those variations were consistent with alternate splicing events [6].

Anatomical context of GBF1


Associations of GBF1 with chemical compounds

  • Using three different approaches [expression of an inactive (E794K) GBF1 mutant, expression of the ARF1 (T31N) mutant with decreased affinity for GTP and Brefeldin A treatment], we show that GBF1 is stabilized on membranes when in a complex with ARF-GDP [7].
  • The interacting domains were mapped to the proline-rich region of GBF1 and the head region of p115 [4].
  • Immunofluorescence microscopy of cells treated with nocodazole or incubated at 15 degrees C has suggested that GBF1 behaves similarly to proteins recycling between the cis-Golgi and the endoplasmic reticulum [8].

Physical interactions of GBF1

  • Recently, we elucidated the underlying mechanism by showing that CVB3 3A interferes with ADP-ribosylation factor 1 (Arf1)-dependent COP-I recruitment to membranes by binding and inhibiting the function of GBF1, a guanine nucleotide exchange factor that is required for the activation of Arf1 (E. Wessels et al., Dev. Cell 11:191-201, 2006) [1].

Other interactions of GBF1

  • Like ARF and coatomer, GBF1 peripherally associates with membranes [7].
  • The trafficking of transmembrane proteins through the existing pathway requires GBF1-mediated ARF activation and COPI recruitment [10].

Analytical, diagnostic and therapeutic context of GBF1

  • Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1 [7].
  • Immunoelectron microscopy has revealed that GBF1 localizes primarily to vesicular and tubular structures apposed to the cis-face of Golgi stacks and minor fractions to the Golgi stacks [8].
  • These splice variants behaved like GBF1 in biological assays based on the observation that GBF1 is cytotoxic at high levels but will confer resistance to BFA when moderately overexpressed [6].


  1. Effects of Picornavirus 3A Proteins on Protein Transport and GBF1-Dependent COP-I Recruitment. Wessels, E., Duijsings, D., Lanke, K.H., van Dooren, S.H., Jackson, C.L., Melchers, W.J., van Kuppeveld, F.J. J. Virol. (2006) [Pubmed]
  2. GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. Claude, A., Zhao, B.P., Kuziemsky, C.E., Dahan, S., Berger, S.J., Yan, J.P., Armold, A.D., Sullivan, E.M., Melançon, P. J. Cell Biol. (1999) [Pubmed]
  3. Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the Golgi. Niu, T.K., Pfeifer, A.C., Lippincott-Schwartz, J., Jackson, C.L. Mol. Biol. Cell (2005) [Pubmed]
  4. The membrane-tethering protein p115 interacts with GBF1, an ARF guanine-nucleotide-exchange factor. García-Mata, R., Sztul, E. EMBO Rep. (2003) [Pubmed]
  5. ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1. García-Mata, R., Szul, T., Alvarez, C., Sztul, E. Mol. Biol. Cell (2003) [Pubmed]
  6. Characterization of alternatively spliced and truncated forms of the Arf guanine nucleotide exchange factor GBF1 defines regions important for activity. Claude, A., Zhao, B.P., Melançon, P. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  7. Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1. Szul, T., Garcia-Mata, R., Brandon, E., Shestopal, S., Alvarez, C., Sztul, E. Traffic (2005) [Pubmed]
  8. GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat. Kawamoto, K., Yoshida, Y., Tamaki, H., Torii, S., Shinotsuka, C., Yamashina, S., Nakayama, K. Traffic (2002) [Pubmed]
  9. Human GBF1 is a ubiquitously expressed gene of the sec7 domain family mapping to 10q24. Mansour, S.J., Herbrick, J.A., Scherer, S.W., Melançon, P. Genomics (1998) [Pubmed]
  10. Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking. Szul, T., Grabski, R., Lyons, S., Morohashi, Y., Shestopal, S., Lowe, M., Sztul, E. J. Cell. Sci. (2007) [Pubmed]
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