Reactome | GBF1 recruits ARF:GDP to the ERGIC

GBF1 recruits ARF:GDP to the ERGIC

Stable Identifier

R-HSA-6807866

Type

Reaction [binding]

Species

Homo sapiens

Compartment

endoplasmic reticulum-Golgi intermediate compartment membrane

ReviewStatus

5/5

Locations in the PathwayBrowser

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Metabolism of proteins (Homo sapiens)

- Post-translational protein modification (Homo sapiens)
  - Asparagine N-linked glycosylation (Homo sapiens)
    - Transport to the Golgi and subsequent modification (Homo sapiens)
      - ER to Golgi Anterograde Transport (Homo sapiens)
        
        COPI-mediated anterograde transport (Homo sapiens)
        
        GBF1 recruits ARF:GDP to the ERGIC (Homo sapiens)

General

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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
22013193	COPII and COPI traffic at the ER-Golgi interface Szul, T, Sztul, E	Physiology (Bethesda)	2011
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
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