The ADP-ribosylation factor GTPase-activating protein GIo3p is involved in ER retrieval

Dogic, Dagmar; Chassey, Benoı̂t de; Pick, Elah; Cassel, Dan; Lefkir, Yaya; Hennecke, Silke; Cosson, Pierre; Letourneur, François

doi:10.1016/s0171-9335(99)80064-8

Cited by 40 publications

(40 citation statements)

References 29 publications

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“…As GEFs and GTPase-activating proteins (GAPs), many proteins have been identified from mammals and yeast (Jackson and Casanova, 2000;Donaldson, 2000). In S. cerevisiae, at least four Arf GEFs, Gea1p, Gea2p, Sec7p, and Syt1p (Peyroche et al, 1996;Sata et al, 1998;Jones et al, 1999), and six putative Arf GAPs, Gcs1p, Glo3p, Sat1p, Sat2p, Sps18p, and Gts1p (Ireland et al, 1994;Poon et al, 1996Poon et al, , 1999Zhang et al, 1998;Dogic et al, 1999) exist. Mutations of these genes give different phenotypes, suggesting that these GEFs and GAPs act on Arf1p at different times and at different places.…”

Section: Regulation Of Multiple Functions Of Arf1pmentioning

confidence: 99%

“…After we submitted the original manuscript of this paper, Eugster et al (2000) showed that COPI subunits (Sec21p and Sec27p) interact with the Arf-GAP Glo3p but not Gcs1p, whereas both Glo3p and Gcs1p have the GAP activity on Arf1p in vitro and interact with the GTP-stabilized mutant Q71L-Arfp in vivo. Dogic et al (1999) showed in the analysis of deletions of the six Arf-GAP genes that ⌬glo3 alone results in a defect in the retrieval of KKXXproteins from the Golgi. These reports support the view that different Arf-GAPs (and Arf-GEFs) act on Arf differently.…”

Section: Regulation Of Multiple Functions Of Arf1pmentioning

confidence: 99%

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Multiple Roles of Arf1 GTPase in the Yeast Exocytic and Endocytic Pathways

Yahara

Ueda

Sato

et al. 2001

MBoC

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ADP-ribosylation factors, a family of small GTPases, are believed to be key regulators of intracellular membrane traffic. However, many biochemical in vitro experiments have led to different models for their involvement in various steps of vesicular transport, and their precise role in living cells is still unclear. We have taken advantage of the powerful yeast genetic system and screened for temperature-sensitive (ts) mutants of the ARF1 gene from Saccharomyces cerevisiae. By random mutagenesis of the whole open reading frame of ARF1 by error-prone PCR, we isolated eight mutants and examined their phenotypes. arf1 ts mutants showed a variety of transport defects and morphological alterations in an allele-specific manner. Furthermore, intragenic complementation was observed between certain pairs of mutant alleles, both for cell growth and intracellular transport. These results demonstrate that the single Arf1 protein is indeed involved in many different steps of intracellular transport in vivo and that its multiple roles may be dissected by the mutant alleles we constructed.

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Section: Regulation Of Multiple Functions Of Arf1pmentioning

confidence: 99%

Section: Regulation Of Multiple Functions Of Arf1pmentioning

confidence: 99%

Multiple Roles of Arf1 GTPase in the Yeast Exocytic and Endocytic Pathways

Yahara

Ueda

Sato

et al. 2001

MBoC

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“…Sec7p is a Golgi-localized protein that is involved in the ER-Golgi and intra-Golgi transport pathways (Franzusoff et al, 1991(Franzusoff et al, , 1992. On the other hand, Gcs1p, Glo3p, Age1p, and Age2p have been identified as Arf GAPs in S. cerevisiae (Zhang et al, 2003;Poon et al, 2001;Dogic et al, 1999;Poon et al, 1996). Gcs1p functions redundantly with Glo3p in the Golgi-to-ER retrograde transport pathway (Poon et al, 1999), and with Age2p in transport from the TGN (Poon et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

The Functional Relationship between the Cdc50p-Drs2p Putative Aminophospholipid Translocase and the Arf GAP Gcs1p in Vesicle Formation in the Retrieval Pathway from Yeast Early Endosomes to the TGN

Sakane

Yamamoto

Tanaka

2006

Cell Struct. Funct.

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ABSTRACT. Drs2p, the catalytic subunit of the Cdc50p-Drs2p putative aminophospholipid translocase, has been implicated in conjunction with the Arf1 signaling pathway in the formation of clathrin-coated vesicles (CCVs) from the TGN. Herein, we searched for Arf regulator genes whose mutations were synthetically lethal with cdc50∆, and identified the Arf GAP gene GCS1. Most of the examined transport pathways in the Cdc50p-depleted gcs1∆ mutant were nearly normal, including endocytic transport to vacuoles, carboxypeptidase Y sorting, and the processing and secretion of invertase. In contrast, this mutant exhibited severe defects in the early endosome-to-TGN transport pathway; proteins that are transported via this pathway, such as the v-SNARE Snc1p, the t-SNARE Tlg1p, and the chitin synthase III subunit Chs3p, accumulated in TGN-independent aberrant membrane structures. We extended our analyses to clathrin adaptors, and found that Gga1p/Gga2p and AP-1 were also involved in this pathway. The Cdc50p-depleted gga1∆ gga2∆ mutant and the gcs1∆ apl2∆ (the β1 subunit of AP-1) mutant exhibited growth defects and intracellular Snc1p-containing membranes accumulated in these cells. These results suggest that Cdc50p-Drs2p plays an important role in the Arf1p-mediated formation of CCVs for the retrieval pathway from early endosomes to the TGN.

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“…Several observations suggest that Glo3p is more important than Gcs1p for COPI vesicle formation. First, deletion of Glo3p, in contrast to any other ARFGAP, causes an impairment in retrieval of dilysine-tagged protein from the Golgi to the ER (24). Second, deleting Glo3p has more severe phenotypes on the function of the secretory pathway than that of Gcs1p knockdown (23).…”

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confidence: 99%

ARFGAP2 and ARFGAP3 Are Essential for COPI Coat Assembly on the Golgi Membrane of Living Cells

Kartberg

Asp

Dejgaard

et al. 2010

Journal of Biological Chemistry

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Coat protein complex I (COPI) vesicles play a central role in the recycling of proteins in the early secretory pathway and transport of proteins within the Golgi stack. Vesicle formation is initiated by the exchange of GDP for GTP on ARF1 (ADP-ribosylation factor 1), which, in turn, recruits the coat protein coatomer to the membrane for selection of cargo and membrane deformation. ARFGAP1 (ARF1 GTPase-activating protein 1) regulates the dynamic cycling of ARF1 on the membrane that results in both cargo concentration and uncoating for the generation of a fusion-competent vesicle. Two human orthologues of the yeast ARFGAP Glo3p, termed ARFGAP2 and ARFGAP3, have been demonstrated to be present on COPI vesicles generated in vitro in the presence of guanosine 5-3-O-(thio)triphosphate. Here, we investigate the function of these two proteins in living cells and compare it with that of ARFGAP1. We find that ARFGAP2 and ARFGAP3 follow the dynamic behavior of coatomer upon stimulation of vesicle budding in vivo more closely than does ARFGAP1. Electron microscopy of ARFGAP2 and ARFGAP3 knockdowns indicated Golgi unstacking and cisternal shortening similarly to conditions where vesicle uncoating was blocked. Furthermore, the knockdown of both ARFGAP2 and ARFGAP3 prevents proper assembly of the COPI coat lattice for which ARFGAP1 does not seem to play a major role. This suggests that ARFGAP2 and ARFGAP3 are key components of the COPI coat lattice and are necessary for proper vesicle formation.

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The ADP-ribosylation factor GTPase-activating protein GIo3p is involved in ER retrieval

Cited by 40 publications

References 29 publications

Multiple Roles of Arf1 GTPase in the Yeast Exocytic and Endocytic Pathways

Multiple Roles of Arf1 GTPase in the Yeast Exocytic and Endocytic Pathways

The Functional Relationship between the Cdc50p-Drs2p Putative Aminophospholipid Translocase and the Arf GAP Gcs1p in Vesicle Formation in the Retrieval Pathway from Yeast Early Endosomes to the TGN

ARFGAP2 and ARFGAP3 Are Essential for COPI Coat Assembly on the Golgi Membrane of Living Cells

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