Differences between AGAP1, ASAP1 and Arf GAP1 in substrate recognition: interaction with the N-terminus of Arf1

Yoon, Hye‐Young; Jacques, Kerry M.; NEALON, B; Stauffer, Stacey; Premont, Richard T.; ARANDAZZO, P

doi:10.1016/s0898-6568(04)00026-9

Cited by 26 publications

(33 citation statements)

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“…His-Brag2 Sec7-PH , His-(K753S,K756S)Brag2 Sec7-PH , His-(R762S)Brag2 Sec7-PH , His-Brag2 Sec7-linker , and His-Brag2 Sec7 were expressed in bacteria and purified using a His-Trap HP column followed by a Hiload16/60 Superdex 75 column (GE Healthcare). The expression and purification of myristoylated Arf1 (myrArf1), (L8K)Arf1, and (⌬17)Arf1 have been described previously (13)(14)(15)(16)(17).…”

Section: Protein Preparationsmentioning

confidence: 99%

“…This mutant is not myristoylated, eliminating the possibility that the myristate could account for the observed effects. In addition, (L8K)Arf1 binds GTP independently of lipids, and neither (L8K)Arf1⅐GDP nor (L8K)Arf1⅐GTP binds to lipids (13,14). Therefore, effects of the membrane on activity could be separated from effects of the membrane on product accumulation.…”

Section: Ph Domain and Interdomain Linker Promote Activity Of Sec7 Domentioning

confidence: 99%

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The Pleckstrin Homology (PH) Domain of the Arf Exchange Factor Brag2 Is an Allosteric Binding Site

Jian

Gruschus

Sztul

et al. 2012

Journal of Biological Chemistry

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Background: Brag2 is a PH domain-containing Arf guanine nucleotide exchange factor (GEF) that regulates cell adhesion. Results: PIP 2 association with the PH domain stimulated Brag2 activity. Regulation was dependent on the N terminus of Arf and independent of the N-terminal myristate. Conclusion: PIP 2 binding to the PH domain allosterically modifies Brag2 activity. Significance: A novel regulatory mechanism for GEFs was identified.

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Section: Protein Preparationsmentioning

confidence: 99%

Section: Ph Domain and Interdomain Linker Promote Activity Of Sec7 Domentioning

confidence: 99%

The Pleckstrin Homology (PH) Domain of the Arf Exchange Factor Brag2 Is an Allosteric Binding Site

Jian

Gruschus

Sztul

et al. 2012

Journal of Biological Chemistry

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“…Based on the finding that Arf1, but not Arf6 was required for retrograde transport to the TGN, we performed sulfation analysis on intact cells that were transfected with validated siRNAs pools (except SMAP2) against six ArfGAPs with preferential GAP activity on Arf1 (Miura et al, 2002;Natsume et al, 2006;Nie et al, 2005;Vitale et al, 2000;Yoon et al, 2004). The depletion of the individual proteins was not assayed, and negative results can therefore not be interpreted.…”

Section: Identification Of Arfgap Proteins That Function In Retrogradmentioning

confidence: 99%

AGAP2 regulates retrograde transport between early endosomes and the TGN

Shiba

Römer

Mardones

et al. 2010

Journal of Cell Science

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SummaryThe retrograde transport route links early endosomes and the TGN. Several endogenous and exogenous cargo proteins use this pathway, one of which is the well-explored bacterial Shiga toxin. ADP-ribosylation factors (Arfs) are ~20 kDa GTP-binding proteins that are required for protein traffic at the level of the Golgi complex and early endosomes. In this study, we expressed mutants and protein fragments that bind to Arf-GTP to show that Arf1, but not Arf6 is required for transport of Shiga toxin from early endosomes to the TGN. We depleted six Arf1-specific ARF-GTPase-activating proteins and identified AGAP2 as a crucial regulator of retrograde transport for Shiga toxin, cholera toxin and the endogenous proteins TGN46 and mannose 6-phosphate receptor. In AGAP2-depleted cells, Shiga toxin accumulates in transferrin-receptor-positive early endosomes, suggesting that AGAP2 functions in the very early steps of retrograde sorting. A number of other intracellular trafficking pathways are not affected under these conditions. These results establish that Arf1 and AGAP2 have key trafficking functions at the interface between early endosomes and the TGN.

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“…A truncated form of Arf1 ([⌬17]Arf1) that differs from full-length Arf1 in that it is soluble when bound to GTP (Randazzo et al, 1994) and, although a poor substrate for Arf GAPs (Yoon et al, 2004), it is easier to handle in kinetic studies. When this is used as a substrate for truncated Arf GAP1, COPI accelerates GTP hydrolysis.…”

Section: Arf Gaps In the Classical Modelmentioning

confidence: 99%

Arf GAPs and membrane traffic

Nie

Randazzo

2006

Journal of Cell Science

125

128

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The selective transfer of material between membrane-delimited organelles is mediated by protein-coated vesicles. In many instances, formation of membrane trafficking intermediates is regulated by the GTP-binding protein Arf. Binding and hydrolysis of GTP by Arf was originally linked to the assembly and disassembly of vesicle coats. Arf GTPase-activating proteins (GAPs), a family of proteins that induce hydrolysis of GTP bound to Arf, were therefore proposed to regulate the disassembly and dissociation of vesicle coats. Following the molecular identification of Arf GAPs, the roles for GAPs and GTP hydrolysis have been directly examined. GAPs have been found to bind cargo and known coat proteins as well as directly contribute to vesicle formation, which is consistent with the idea that GAPs function as subunits of coat proteins rather than simply Arf inactivators. In addition, GTP hydrolysis induced by GAPs occurs largely before vesicle formation and is required for sorting. These results are the primary basis for modifications to the classical model for the function of Arf in transport vesicle formation, including a recent proposal that Arf has a proofreading, rather than a structural, role.

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Differences between AGAP1, ASAP1 and Arf GAP1 in substrate recognition: interaction with the N-terminus of Arf1

Cited by 26 publications

References 0 publications

The Pleckstrin Homology (PH) Domain of the Arf Exchange Factor Brag2 Is an Allosteric Binding Site

The Pleckstrin Homology (PH) Domain of the Arf Exchange Factor Brag2 Is an Allosteric Binding Site

AGAP2 regulates retrograde transport between early endosomes and the TGN

Arf GAPs and membrane traffic

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