GBF1 recruits ARF:GDP to the ERGIC

Stable Identifier
R-HSA-6807866
Type
Reaction [binding]
Species
Homo sapiens
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GBF1 recruits inactive ARF:GDP complexes to the ERGIC (Monetta et al, 2007). There are 5 known ADP-ribosylation factor proteins (ARFs) in the human cell. Class I members ARF1 and ARF 3 are expressed at high levels and broadly distributed through the secretory system, while Class II members ARF4 and ARF5 are expressed at lower levels, with ARF4 showing the most specific localization to the ERGIC compartment. ARF6, the single Class III ARF, appears to function more specifically in endocytosis and actin dynamics (Chun et al, 2008; reviewed in D'Souza-Schorey and Chavrier, 2006; Szul and Sztul, 2011). There is conflicting evidence regarding what ARF(s) is required at the ERGIC membrane. GBF1 has been shown to activate ARF1, 4, and 5, but not ARF3, while single and pairwise knockdown of ARF1, 3, 4 and 5 suggests that although no single ARF is responsible for any given step in the secretory pathway, ARF1 and ARF3 contribute most specifically to the ERGIC-Golgi step (Manolea et al, 2010; Volpicelli-Daley et al, 2005). Recruitment of ARF at may also be facilitated by interaction with p24 family members (Gommel et al, 2001; reviewed in Schuiki and Volchuk, 2012).

Literature References
PubMed ID Title Journal Year
18524849 Characterization of class I and II ADP-ribosylation factors (Arfs) in live cells: GDP-bound class II Arfs associate with the ER-Golgi intermediate compartment independently of GBF1

Chun, J, Shapovalova, Z, Dejgaard, SY, Presley, JF, Melançon, P

Mol. Biol. Cell 2008
22013193 COPII and COPI traffic at the ER-Golgi interface

Szul, T, Sztul, E

Physiology (Bethesda) 2011
20357002 Arf3 is activated uniquely at the trans-Golgi network by brefeldin A-inhibited guanine nucleotide exchange factors

Manolea, F, Chun, J, Chen, DW, Clarke, I, Summerfeldt, N, Dacks, JB, Melançon, P

Mol. Biol. Cell 2010
17429068 Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI association

Monetta, P, Slavin, I, Romero, N, Alvarez, C

Mol. Biol. Cell 2007
11726511 Recruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23

Gommel, DU, Memon, AR, Heiss, A, Lottspeich, F, Pfannstiel, J, Lechner, J, Reinhard, C, Helms, JB, Nickel, W, Wieland, FT

EMBO J. 2001
25436559 Diverse roles for the p24 family of proteins in eukaryotic cells

Schuiki, I, Volchuk, A

Biomol Concepts 2012
16030262 Isoform-selective effects of the depletion of ADP-ribosylation factors 1-5 on membrane traffic

Volpicelli-Daley, LA, Li, Y, Zhang, CJ, Kahn, RA

Mol. Biol. Cell 2005
16633337 ARF proteins: roles in membrane traffic and beyond

D'Souza-Schorey, C, Chavrier, P

Nat. Rev. Mol. Cell Biol. 2006
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