Brefeldin A-inhibited guanine nucleotide-exchange activity of Sec7 domain from yeast Sec7 with yeast and mammalian ADP ribosylation factors

Sata, Makoto; Donaldson, Julie G.; Moss, Joel; Vaughan, Martha

doi:10.1073/pnas.95.8.4204

Cited by 88 publications

(80 citation statements)

References 40 publications

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“…7c) as observed in the presence of Arf1[T31N] (Fig. 6A, c1-c4), suggesting that, as in animal cells, Arf1 may play a role in the trafficking of H ϩ -ATPase:GFP to the plasma membrane through a BFA-sensitive factor (Sata et al, 1998;Morinaga et al, 1999).…”

Section: Arf1[t31n] May Cause Fusion Of the Golgi Membranes To The Ermentioning

confidence: 70%

“…In animal cells, BFA and the dominant negative mutant of Arf1 have been shown to have similar effects on intracellular trafficking (Sata et al, 1998;Morinaga et al, 1999). BFA has also been shown to inhibit intracellular trafficking in plant cells (Gomez and Chrispeels, 1993;Boevink et al, 1999).…”

Section: Arf1[t31n] May Cause Fusion Of the Golgi Membranes To The Ermentioning

confidence: 99%

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ADP-Ribosylation Factor 1 of Arabidopsis Plays a Critical Role in Intracellular Trafficking and Maintenance of Endoplasmic Reticulum Morphology in Arabidopsis

Lee¹,

Min

Lee³

et al. 2002

Plant Physiology

121

126

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ADP-ribosylation factors (Arf), a family of small GTP-binding proteins, play important roles in intracellular trafficking in animal and yeast cells. Here, we investigated the roles of two Arf homologs, Arf1 and Arf3 of Arabidopsis, in intracellular trafficking in plant cells. We generated dominant negative mutant forms of Arf 1 and Arf3 and examined their effect on trafficking of reporter proteins in protoplasts. Arf1[T31N] inhibited trafficking of H ϩ -ATPase:green fluorescent protein (GFP) and sialyltransferase (ST):GFP to the plasma membrane and the Golgi apparatus. In addition, Arf1[T31N] caused relocalization of the Golgi reporter protein ST:GFP to the endoplasmic reticulum (ER). In protoplasts expressing Arf1[T31N], ST:red fluorescent protein remained in the ER, whereas H ϩ -ATPase:GFP was mistargeted to another organelle. Also, expression of Arf1[T31N] in protoplasts resulted in profound changes in the morphology of the ER. The treatment of protoplasts with brefeldin A had exactly the same effect as Arf1[T31N] on various intracellular trafficking pathways. In contrast, Arf3[T31N] did not affect trafficking of any of these reporter proteins. Inhibition experiments using mutants with various domains swapped between Arf1 and Arf3 revealed that the N-terminal domain is interchangeable for trafficking inhibition. However, in addition to the T31N mutation, motifs in domains II, III, and IV of Arf1 were necessary for inhibition of trafficking of H ϩ -ATPase:GFP. Together, these results strongly suggest that Arf1 plays a role in the intracellular trafficking of cargo proteins in Arabidopsis, and that Arf1 functions through a brefeldin A-sensitive factor.In eukaryotic cells, a large number of proteins are transported to their final destination after translation by a process called intracellular trafficking. The mechanism of intracellular trafficking has been extensively studied in animal, plant, and yeast cells. Based on numerous studies, the general mechanism of intracellular trafficking is thought to be similar in various organisms (Rothman, 1994; Jahn and Sü dhof, 1999; Bassham and Raikhel, 2000), implying that the fundamental aspects of intracellular trafficking between the endoplasmic reticulum (ER), Golgi apparatus, vacuole, and plasma membrane are similar in plant cells as well. In fact, many plant proteins have been shown to complement mutations in corresponding proteins in yeast cells (Bassham et al., 1995; Takeuchi et al., 1998). Also, proteins such as clathrin, coatomer subunits of coat protein I (COPI) vesicles, and many small GTP-binding proteins have been identified in plant cells (Memon et al., 1993; Regad et al., 1993; Lebas and Axelos, 1994; Blackbourn and Jackson, 1996; Contreras et al., 2000), although in most cases, the exact biological roles of these proteins have not been directly addressed. However, differences in trafficking also exist between plant and animal cells. It has recently been shown that plant cells have at least two different types of vacuoles: the lytic and storage vacuoles...

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Section: Arf1[t31n] May Cause Fusion Of the Golgi Membranes To The Ermentioning

confidence: 70%

Section: Arf1[t31n] May Cause Fusion Of the Golgi Membranes To The Ermentioning

confidence: 99%

ADP-Ribosylation Factor 1 of Arabidopsis Plays a Critical Role in Intracellular Trafficking and Maintenance of Endoplasmic Reticulum Morphology in Arabidopsis

Lee¹,

Min

Lee³

et al. 2002

Plant Physiology

121

126

View full text Add to dashboard Cite

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“…GDP-GTP exchange on Arf1 and its paralogs makes use of a common structural motif, the Sec7 domain, named for the late Golgi GEF that is the target of the fungal metabolite, Brefeldin A (Sata et al 1998(Sata et al , 1999. In Golgi-ER retrograde traffic, two redundant GEFs, Gea1 and Gea2, each with a Sec7 domain, likely initiate coat assembly by triggering local recruitment of Arf1 (Peyroche et al 1996;Spang et al 2001).…”

Section: Composition and Structure Of The Copi Coatmentioning

confidence: 99%

Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway

2013

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The secretory pathway is responsible for the synthesis, folding, and delivery of a diverse array of cellular proteins. Secretory protein synthesis begins in the endoplasmic reticulum (ER), which is charged with the tasks of correctly integrating nascent proteins and ensuring correct post-translational modification and folding. Once ready for forward traffic, proteins are captured into ER-derived transport vesicles that form through the action of the COPII coat. COPII-coated vesicles are delivered to the early Golgi via distinct tethering and fusion machineries. Escaped ER residents and other cycling transport machinery components are returned to the ER via COPI-coated vesicles, which undergo similar tethering and fusion reactions. Ultimately, organelle structure, function, and cell homeostasis are maintained by modulating protein and lipid flux through the early secretory pathway. In the last decade, structural and mechanistic studies have added greatly to the strong foundation of yeast genetics on which this field was built. Here we discuss the key players that mediate secretory protein biogenesis and trafficking, highlighting recent advances that have deepened our understanding of the complexity of this conserved and essential process. TABLE OF CONTENTS Abstract 383Introduction 384

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“…To determine if ␣-syn-EGFP vesicular accumulations affect the organization of the Golgi, we examined the localization of RFP-tagged Sec7p, a guanine nucleotide exchange factor that localizes to late Golgi (Sata et al, 1998). In cells expressing EGFP alone, Sec7p was localized to small punctate structures around the periphery of the cell.…”

Section: Vesicular Clustering Caused By ␣-Syn-egfp Expression Disruptmentioning

confidence: 99%

α-Synuclein–induced Aggregation of Cytoplasmic Vesicles inSaccharomyces cerevisiae

Soper¹,

Roy²,

Stieber³

et al. 2008

MBoC

147

168

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Aggregated ␣-synuclein (␣-syn) fibrils form Lewy bodies (LBs), the signature lesions of Parkinson's disease (PD) and related synucleinopathies, but the pathogenesis and neurodegenerative effects of LBs remain enigmatic. Recent studies have shown that when overexpressed in Saccharomyces cerevisiae, ␣-syn localizes to plasma membranes and forms cytoplasmic accumulations similar to human ␣-syn inclusions. However, the exact nature, composition, temporal evolution, and underlying mechanisms of yeast ␣-syn accumulations and their relevance to human synucleinopathies are unknown. Here we provide ultrastructural evidence that ␣-syn accumulations are not comprised of LB-like fibrils, but are associated with clusters of vesicles. Live-cell imaging showed ␣-syn initially localized to the plasma membrane and subsequently formed accumulations in association with vesicles. Imaging of truncated and mutant forms of ␣-syn revealed the molecular determinants and vesicular trafficking pathways underlying this pathological process. Because vesicular clustering is also found in LB-containing neurons of PD brains, ␣-syn-mediated vesicular accumulation in yeast represents a model system to study specific aspects of neurodegeneration in PD and related synucleinopathies. INTRODUCTIONParkinson's disease (PD) is the most prevalent neurodegenerative movement disorder and is characterized by bradykinesia, rigidity, postural instability, and resting tremor (Galvin et al., 2001;Forman et al., 2005), as well as by the loss of dopaminergic neurons and presence of neuronal inclusions, known as Lewy bodies (LBs) and Lewy neurites (Forman et al., 2005). The identification of an ␣-syn gene (SNCA) mutation associated with autosomal dominant PD (Polymeropoulos et al., 1997), and the identification of fibrillar ␣-syn as the principal component of LB pathology (Spillantini et al., 1997), indicate that the LBs formed by ␣-syn define classic PD and are implicated in disease pathogenesis. The subsequent identification of additional disease-linked SNCA mutations (Polymeropoulos et al., 1997;Kruger et al., 1998;Zarranz et al., 2004), as well as replications of the SNCA gene (Singleton et al., 2003;Chartier-Harlin et al., 2004), indicate that both mutant ␣-syn and increased expression of wildtype (WT) ␣-syn can cause neurodegeneration.In addition to PD, filamentous ␣-syn inclusions have been detected in other neurodegenerative diseases including the LB variant of Alzheimer's disease, dementia with LBs, neurodegeneration with brain iron accumulation type-1, and multiple system atrophy, which are collectively known as synucleinopathies (Spillantini et al., 1997;Duda et al., 2000). ␣-syn fibrils exhibit properties of amyloid (Spillantini et al., 1998), and ␣-syn assembles into amyloid fibrils in vitro (Han et al., 1995;Giasson et al., 1999), whereas SNCA mutations can accelerate ␣-syn fibrillization (Conway et al., 1998;Greenbaum et al., 2005). Therefore, it is plausible that ␣-syn misfolds and aggregates into amyloid fibrils that are neurotoxic and play a cau...

show abstract

Brefeldin A-inhibited guanine nucleotide-exchange activity of Sec7 domain from yeast Sec7 with yeast and mammalian ADP ribosylation factors

Cited by 88 publications

References 40 publications

ADP-Ribosylation Factor 1 of Arabidopsis Plays a Critical Role in Intracellular Trafficking and Maintenance of Endoplasmic Reticulum Morphology in Arabidopsis

ADP-Ribosylation Factor 1 of Arabidopsis Plays a Critical Role in Intracellular Trafficking and Maintenance of Endoplasmic Reticulum Morphology in Arabidopsis

Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway

α-Synuclein–induced Aggregation of Cytoplasmic Vesicles inSaccharomyces cerevisiae

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