ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

Shiba, Yoko; Luo, Ruibai; Hinshaw, Jenny E.; Szul, Tomasz; Hayashi, Ryo; Sztul, Elizabeth; Nagashima, Kunio; Baxa, Ulrich; Randazzo, Paul A.

doi:10.4161/cl.1.4.18896

Cited by 20 publications

(27 citation statements)

References 76 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Previous studies have established that ArfGAP1 localizes to the Golgi where it promotes GTP hydrolysis on Arfs (Cukierman et al, 1995;Szafer et al, 2001;Shiba et al, 2011). Further characterization of the N-terminal GAP domain identified a crucial 'arginine finger' residue that participates in catalysis (Szafer et al, 2000;Ismail et al, 2010), and mutation of this arginine residue (residue 50 in human ArfGAP1) abrogated GAP activity in vivo (Shiba et al, 2011). To examine the potential role that the ratio of Arf-GDP to Arf-GTP played in GBF1 recruitment, we examined the distribution of endogenous GBF1 in HeLa cells transiently expressing low levels of EGFP-tagged wild-type (WT) or the catalytically dead R50Q point GAP1.…”

Section: Treatment Of Hela Cells With 200 MMmentioning

confidence: 99%

Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1

Quilty

Gray

Summerfeldt

et al. 2013

Journal of Cell Science

View full text Add to dashboard Cite

ADP-ribosylation factors (Arfs) play central roles in the regulation of vesicular trafficking through the Golgi. Arfs are activated at the Golgi membrane by guanine-nucleotide-exchange factors (GEFs) that are recruited from cytosol. Here, we describe a novel mechanism for the regulation of recruitment and activity of the ArfGEF Golgi-specific BFA resistance factor 1 (GBF1). Conditions that alter the cellular Arf-GDP:Arf-GTP ratio result in GBF1 recruitment. This recruitment of GBF1 occurs selectively on cis-Golgi membranes in direct response to increased Arf-GDP. GBF1 recruitment requires Arf-GDP myristoylation-dependent interactions suggesting regulation of a membrane-bound factor. Once recruited, GBF1 causes increased Arf-GTP production at the Golgi, consistent with a feed-forward selflimiting mechanism of Arf activation. This mechanism is proposed to maintain steady-state levels of Arf-GTP at the cis-Golgi during cycles of Arf-dependent trafficking events.

show abstract

Section: Treatment Of Hela Cells With 200 MMmentioning

confidence: 99%

Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1

Quilty

Gray

Summerfeldt

et al. 2013

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…However, coat-cargo complex is formed prior to making a vesicle, so that activation of the GAP would also occur prior to vesicle formation. The competing models of the role of Arf and ArfGAPs for the formation of coated vesicles are discussed in more detail in a series of papers published from 2009 to 2011 (Shiba et al, 2011;Hsu, 2011;Hsu et al, 2009;Beck et al, 2009b;Beck et al, 2009a). Importantly, the enzymology has been found valuable to gain insights into biological processes.…”

Section: E Esmentioning

confidence: 99%

“…ArfGAP1 was the first identified ArfGAP and the first GAP found to regulate membrane traffic, although its precise role remains unknown (Hsu, 2011;Hsu et al, 2009;Kahn, 2009;East and Kahn, 2011;Kahn, 2011;Beck et al, 2011;Weimer et al, 2008;Beck et al, 2009b;Shiba et al, 2011;Spang et al, 2010). The protein is approximately 50 kDa with the Arf GAP domain at the N-terminus and a unique C-terminus that contains two ALPS motifs that are described below.…”

Section: Arfgap1 2 and 3: Control By Two Interacting Proteinsmentioning

confidence: 99%

Enzymology and Regulation of ArfGAPs and ArfGEFs

Zhai¹,

Jian²,

Luo³

et al. 2012

Crosstalk and Integration of Membrane Trafficking Pathways

Self Cite

View full text Add to dashboard Cite

“…The authors suggested that the biological role of Gcs1 is a downstream effector of Arfs, rather than a downregulator. In mammalian cells, overexpression of ArfGAP1 produces more vesicles, rather than inhibiting transport [19]. The depletion of ACAP3, the ArfGAP for Arf6, resulted in the inhibition of neurite outgrowth [32].…”

Section: Arfgaps; Depletion or Overexpression?mentioning

confidence: 99%

“…In the presence of COPI and cargo, GAP activity of ArfGAP1 increases and hydrolyzes Arf•GTP [18]. Arf•GDP is released from the membrane and ArfGAP1 promotes polymerization of COPI to produce COPI coated vesicles [19]. In this model, GTP hydrolysis is required for determining if the interaction between COPI and its specific cargo is taking place ( Figure 2 step 4 and 5).…”

Section: Introductionmentioning

confidence: 99%

ArfGAPs; Depletion or Overexpression?

Shiba¹

2017

Res Rev Insights

Self Cite

View full text Add to dashboard Cite

Arf proteins are small GTP binding proteins that regulate intracellular traffic, actin remodeling and lipid metabolism. In the GTP-bound state, Arf is thought to be an active form that can bind to organelle membranes and many effectors. Arf in the GDP-bound state is thought to be an inactive form and released to cytosol. Arf GTPase Activating Proteins (ArfGAPs) hydrolyze Arf•GTP to Arf·GTP. Because GAPs "inactivate" small GTPases, the research of GAPs has often been done by overexpression of the GAPs looking at the biological consequences of the overexpression. However, decades of study about ArfGAP1 in COPI coated vesicle formation has led to a molecular model by which ArfGAP1 plays a role in fidelity of cargo sorting. This model implies that a deletion experiment would be appropriate to analyze the function of ArfGAP family proteins, rather than overexpression. Here, I briefly describe the role of ArfGAP1 in COPI coated vesicle formation, and discuss the biological consequences of depletion of ArfGAPs.

show abstract

ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization

Cited by 20 publications

References 76 publications

Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1

Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1

Enzymology and Regulation of ArfGAPs and ArfGEFs

ArfGAPs; Depletion or Overexpression?

Contact Info

Product

Resources

About