Mechanisms of COPI vesicle formation

Hsu, Victor; Yang, Jia‐Shu

doi:10.1016/j.febslet.2009.10.056

Cited by 42 publications

(41 citation statements)

References 60 publications

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“…Activation of ADP ribosylation factor 1 (ARF1) is required for the recruitment of COPI complex onto the Golgi membranes (36). In ARF1 siRNA-treated cells infected with VSV, the viral gene expression was reduced by twofold with concomitant similar reduction in the levels of ARF1 protein ( Fig.…”

Section: Copi Is Necessary For Vsv Infection At the Level Of Viral Genementioning

confidence: 95%

RNAi screening reveals requirement for host cell secretory pathway in infection by diverse families of negative-strand RNA viruses

Panda

Das

Dinh

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Negative-strand (NS) RNA viruses comprise many pathogens that cause serious diseases in humans and animals. Despite their clinical importance, little is known about the host factors required for their infection. Using vesicular stomatitis virus (VSV), a prototypic NS RNA virus in the family Rhabdoviridae, we conducted a human genomewide siRNA screen and identified 72 host genes required for viral infection. Many of these identified genes were also required for infection by two other NS RNA viruses, the lymphocytic choriomeningitis virus of the Arenaviridae family and human parainfluenza virus type 3 of the Paramyxoviridae family. Genes affecting different stages of VSV infection, such as entry/uncoating, gene expression, and assembly/release, were identified. Depletion of the proteins of the coatomer complex I or its upstream effectors ARF1 or GBF1 led to detection of reduced levels of VSV RNA. Coatomer complex I was also required for infection of lymphocytic choriomeningitis virus and human parainfluenza virus type 3. These results highlight the evolutionarily conserved requirements for gene expression of diverse families of NS RNA viruses and demonstrate the involvement of host cell secretory pathway in the process.RNA interference | transcription and replication | host cell factors for virus infection

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Section: Copi Is Necessary For Vsv Infection At the Level Of Viral Genementioning

confidence: 95%

RNAi screening reveals requirement for host cell secretory pathway in infection by diverse families of negative-strand RNA viruses

Panda

Das

Dinh

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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“…To maintain organelle homeostasis, the flow of membranes and proteins between the ER and Golgi has to be balanced. COPIcoated vesicles retrieve ER-resident proteins from the Golgi and the ER-Golgi intermediate compartment (ERGIC) and release them back into the ER (reviewed by Hsu and Yang, 2009). The formation of both COPII-and COPI-coated vesicles is regulated by G-proteins of the ARF/SAR superfamily (reviewed by Gillingham and Munro, 2007).…”

Section: Introductionmentioning

confidence: 99%

The Drosophila Sec7 domain guanine nucleotide exchange factor protein Gartenzwerg localizes at the cis-Golgi and is essential for epithelial tube expansion

Armbruster¹,

Luschnig²

2012

Development

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Protein trafficking through the secretory pathway plays a key role in epithelial organ development and function. The expansion of tracheal tubes in Drosophila depends on trafficking of coatomer protein complex I (COPI)-coated vesicles between the Golgi complex and the endoplasmic reticulum (ER). However, it is not clear how this pathway is regulated. Here we describe an essential function of the Sec7 domain guanine nucleotide exchange factor (GEF) gartenzwerg (garz) in epithelial tube morphogenesis and protein secretion. garz is essential for the recruitment of COPI components and for normal Golgi organization. A GFP-Garz fusion protein is distributed in the cytoplasm and accumulates at the cis-Golgi. Localization to the Golgi requires the C-terminal part of Garz. Conversely, blocking the GDP-GTP nucleotide exchange reaction leads to constitutive Golgi localization, suggesting that Garz cycles in a GEF-activitydependent manner between cytoplasmic and Golgi-membrane-localized pools. The related human ARF-GEF protein GBF1 can substitute for garz function in Drosophila tracheal cells, indicating that the relevant functions of these proteins are conserved. We show that garz interacts genetically with the ARF1 homolog ARF79F and with the ARF1-GAP homolog Gap69C, thus placing garz in a regulatory circuit that controls COPI trafficking in Drosophila. Interestingly, overexpression of garz causes accumulation of secreted proteins in the ER, suggesting that excessive garz activity leads to increased retrograde trafficking. Thus, garz might regulate epithelial tube morphogenesis and secretion by controlling the rate of trafficking of COPI vesicles. Summary Protein trafficking through the secretory pathway plays a key role in epithelial organ development and function. The expansion of tracheal tubes in Drosophila depends on trafficking of coatomer protein complex I (COPI)-coated vesicles between the Golgi complex and the endoplasmic reticulum (ER). However, it is not clear how this pathway is regulated. Here we describe an essential function of the Sec7 domain guanine nucleotide exchange factor (GEF) gartenzwerg (garz) in epithelial tube morphogenesis and protein secretion. garz is essential for the recruitment of COPI components and for normal Golgi organization. A GFP-Garz fusion protein is distributed in the cytoplasm and accumulates at the cis-Golgi. Localization to the Golgi requires the C-terminal part of Garz. Conversely, blocking the GDP-GTP nucleotide exchange reaction leads to constitutive Golgi localization, suggesting that Garz cycles in a GEF-activitydependent manner between cytoplasmic and Golgi-membrane-localized pools. The related human ARF-GEF protein GBF1 can substitute for garz function in Drosophila tracheal cells, indicating that the relevant functions of these proteins are conserved. We show that garz interacts genetically with the ARF1 homolog ARF79F and with the ARF1-GAP homolog Gap69C, thus placing garz in a regulatory circuit that controls COPI trafficking in Drosophila. Interestingly, ov...

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“…There are nine different COPI complex subunits: ␣, ␤1, ␤2, ␦, ε, ␥1, ␥2, 1, and 2. Each COPI complex contains a single copy of the ␣, ␤1, ␤2, ␦, and ε subunits in addition to one of the following isoform combinations: ␥1/1, ␥1/2, or ␥2/1 (15)(16)(17). Together, COPI complexes form a vesicle coat that traffics contents between Golgi stacks and cargoes between the Golgi apparatus and the endoplasmic reticulum (ER) (15,17,18).…”

mentioning

confidence: 99%

Dissecting the Role of COPI Complexes in Influenza Virus Infection

Sun

Zhuang

2013

J Virol

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As an obligate pathogen, influenza virus requires host cell factors and compartments to mediate productive infection and to produce infectious progeny virus. Recently, several small interfering RNA (siRNA) knockdown screens revealed influenza virus host dependency proteins, all of which identified at least two subunits of the coat protein I (COPI) complex. COPI proteins oligomerize to form coated vesicles that transport contents between the Golgi apparatus and the endoplasmic reticulum, and they have also been reported to mediate endosomal trafficking. However, it remains unclear which steps in the influenza virus infection cycle rely on the COPI complex. Upon systematic dissection of the influenza virus infection cycle, from entry to progeny virion production, we found that prolonged exposure to COPI complex disruption through siRNA depletion resulted in significant defects in virus internalization and trafficking to late endosomes. Acute inhibition of COPI complex recruitment to the Golgi apparatus with pharmacological compounds failed to recapitulate the same entry defects as observed with the COPI-depleted cells but did result in specific decreases in viral membrane protein expression and assembly, leading to defects in progeny virion production. Taken together, our findings suggest that COPI complexes likely function indirectly in influenza virus entry but play direct roles in viral membrane protein expression and assembly.

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Mechanisms of COPI vesicle formation

Cited by 42 publications

References 60 publications

RNAi screening reveals requirement for host cell secretory pathway in infection by diverse families of negative-strand RNA viruses

RNAi screening reveals requirement for host cell secretory pathway in infection by diverse families of negative-strand RNA viruses

The Drosophila Sec7 domain guanine nucleotide exchange factor protein Gartenzwerg localizes at the cis-Golgi and is essential for epithelial tube expansion

Dissecting the Role of COPI Complexes in Influenza Virus Infection

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