OsAGAP, an ARF‐GAP from rice, regulates root development mediated by auxin in Arabidopsis

Zhuang, Xiaolei; Xu, Yunyuan; Chong, Kang; Lan, Lefu; Xue, Yongbiao; Xu, Zhi-Hong

doi:10.1111/j.1365-3040.2004.01253.x

Cited by 31 publications

(31 citation statements)

References 62 publications

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“…To monitor in vitro GTP hydrolysis by His-LeoA and HisLeoADG, 1 mg purified protein was added to the Enzchek Phosphate assay kit (Molecular Probes), which provides a sensitive GTPase assay system used previously to study the activity of a related family of GTPases (Zhuang et al, 2005). GTP hydrolysis was assayed every 15 s for 5 min by measuring the change in absorbance at 360 nm (Fig.…”

Section: Leoa Is a Gtpasementioning

confidence: 99%

Biochemical characterization of the enterotoxigenic Escherichia coli LeoA protein

Brown

Hardwidge

2007

Microbiology

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Enterotoxigenic Escherichia coli (ETEC) causes enterotoxin-induced diarrhoea and significant mortality. The molecular mechanisms underlying how the heat-labile enterotoxin (LT) is secreted during infection are poorly understood. ETEC produce outer-membrane vesicles (OMVs) containing LT that are endocytosed into host cells. Although OMV production and protein content may be a regulated component of ETEC pathogenesis, how LT loading into OMVs is regulated is unknown. The LeoA protein plays a role in secreting LT from the bacterial periplasm. To begin to understand the function of LeoA and its role in ETEC H10407 pathogenesis, a site-directed mutant lacking the putative GTP-binding domain was constructed. The ability of wild-type and mutant LeoA to hydrolyse GTP in vitro was quantified. This domain was found to be responsible for GTP binding; it is important to LeoA's function in LT secretion, and may play a modest role in the formation and protein content of OMVs. Deletion of leoA reduced the abundance of OmpX in outer-membrane protein preparations and of LT in OMVs. Immunoprecipitation experiments revealed that LeoA interacts directly with OmpA, but that the GTP-binding domain is nonessential for this interaction. Deletion of leoA rendered ETEC H10407 non-motile, through apparent periplasmic accumulation of FliC.

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Section: Leoa Is a Gtpasementioning

confidence: 99%

Biochemical characterization of the enterotoxigenic Escherichia coli LeoA protein

Brown

Hardwidge

2007

Microbiology

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“…Supporting this is that numerous proteins with GAP and sec7 domains have been identified by sequence analysis of the entire Arabidopsis (Arabidopsis thaliana) genome (Vernoud et al, 2003;Memon, 2004). However, of these large numbers of proteins, only a few have been studied in detail (Steinmann et al, 1999;Jensen et al, 2000;Koizumi et al, 2005;Zhuang et al, 2005;Sieburth et al, 2006). Arabidopsis ZAC, a protein that bears homology to the GAP domain of Arf GAPs, can activate the GTPase activity of Arf1 in vitro.…”

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confidence: 99%

“…In addition, several mutants have been identified that have mutations in the genes encoding Arf GAPs. These mutants displayed various phenotypes, such as a defect in auxin efflux and vein patterning, indicating that Arf GAPs play a role in these functions (Koizumi et al, 2005;Zhuang et al, 2005;Sieburth et al, 2006).…”

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Overexpression of Arabidopsis AGD7 Causes Relocation of Golgi-Localized Proteins to the Endoplasmic Reticulum and Inhibits Protein Trafficking in Plant Cells

et al. 2007

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“…The physiological roles of some of these AGD isoforms have been demonstrated through their mutant phenotypes: agd3/van3/sfc, nev/ agd5, and rpa/agd10 displayed defects in vein formation, floral organ shedding, and the growth of root hairs and pollen tubes, respectively (Koizumi et al, 2005;Sieburth et al, 2006;Song et al, 2006;Min et al, 2007;Yoo et al, 2008;Hwang and Robinson, 2009). In rice (Oryza sativa), OsAGAP is involved in vein patterning and root development (Zhuang et al, 2005). However, the functional mechanisms of these AGDs that underlie the observed developmental processes are largely unknown.…”

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confidence: 99%

Recruitment of Arf1-GDP to Golgi by Glo3p-Type ArfGAPs Is Crucial for Golgi Maintenance and Plant Growth

et al. 2012

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ADP-ribosylation factor1 (Arf1), a member of the small GTP-binding proteins, plays a pivotal role in protein trafficking to multiple organelles. In its GDP-bound form, Arf1 is recruited from the cytosol to organelle membranes, where it functions in vesicle-mediated protein trafficking. However, the mechanism of Arf1-GDP recruitment remains unknown. Here, we provide evidence that two Glo3p-type Arf GTPase-activating proteins (ArfGAPs), ArfGAP domain8 (AGD8) and AGD9, are involved in the recruitment of Arf1-GDP to the Golgi apparatus in Arabidopsis (Arabidopsis thaliana). RNA interference plants expressing low levels of AGD8 and AGD9 exhibited abnormal Golgi morphology, inhibition of protein trafficking, and arrest of plant growth and development. In RNA interference plants, Arf1 was poorly recruited to the Golgi apparatus. Conversely, high levels of AGD8 and AGD9 induced Arf1 accumulation at the Golgi and suppressed Golgi disruption and inhibition of vacuolar trafficking that was caused by overexpression of AGD7. Based on these results, we propose that the Glo3p-type ArfGAPs AGD8 and AGD9 recruit Arf1-GDP from the cytosol to the Golgi for Arf1-mediated protein trafficking, which is essential for plant development and growth.

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OsAGAP, an ARF‐GAP from rice, regulates root development mediated by auxin in Arabidopsis

Cited by 31 publications

References 62 publications

Biochemical characterization of the enterotoxigenic Escherichia coli LeoA protein

Biochemical characterization of the enterotoxigenic Escherichia coli LeoA protein

Overexpression of Arabidopsis AGD7 Causes Relocation of Golgi-Localized Proteins to the Endoplasmic Reticulum and Inhibits Protein Trafficking in Plant Cells

Recruitment of Arf1-GDP to Golgi by Glo3p-Type ArfGAPs Is Crucial for Golgi Maintenance and Plant Growth

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