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6. Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphate

Author

Filseck, Joachim Moser von, Čopič, Alenka, Delfosse, Vanessa, Vanni, Stefano, Jackson, Catherine L., Bourguet, William, and Drin, Guillaume

Abstract

In eukaryotic cells, phosphatidylserine (PS) is synthesized in the endoplasmic reticulum (ER) but is highly enriched in the plasma membrane (PM), where it contributes negative charge and to specific recruitment of signaling proteins. This distribution relies on transport mechanisms whose nature remains elusive. Here, we found that the PS transporter Osh6p extracted phosphatidylinositol 4-phosphate (PI4P) and exchanged PS for PI4P between two membranes. We solved the crystal structure of Osh6p:PI4P complex and demonstrated that the transport of PS by Osh6p depends on PI4P recognition in vivo. Finally, we showed that the PI4P-phosphatase Sac1p, by maintaining a PI4P gradient at the ER/PM interface, drove PS transport. Thus, PS transport by oxysterol-binding protein–related protein (ORP)/oxysterol- binding homology (Osh) proteins is fueled by PI4P metabolism through PS/PI4P exchange cycles.

Published
2020

8. A human exchange factor for ARF contains Sec-7- and pleckstrin-homology domains

Author

Chardin, Pierre, Paris, Sonia, Antonny, Bruno, Robineau, Sylviane, Beraud-Dufour, Sophie, Jackson, Catherine L., and Chabre, Marc

Subjects
G proteins -- Physiological aspects, Phosphoinositides -- Physiological aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

The human protein, ARNO, includes Sec7 and carboxy-terminal pleckstrin-homology (PH) domains stimulating guanine-nucleotide exchange on ARF1. The PH domain uses the negatively charged phospholipid vesicles supplemented with phosphatidylinositol biphosphate to mediate an increase in the ARNO exchange activity. Brefeldin A fails to suppress the exchange activity of ARNO. This reveals the presence of a regulatory component, associating with ARNO, which is sensitive to brefeldin A.

Published
1996

9. BFR1, a multicopy suppressor of brefeldin A-induced lethality, is implicated in secretion and nuclear segregation in Saccharomyces cerevisiae

Author

Jackson, Catherine L. and Kepes, Francois

Subjects
Saccharomyces -- Research, Mycotoxins -- Physiological aspects, Biological transport -- Analysis, Biological sciences
Abstract

Inhibition of protein transport out of the Golgi apparatus by Brefeldin A (BRA) leads to the disassembly of organelles in mammalian cells. BFA blocking results in the release of the non-clathrin coat from Golgi vesicles and membranes. The elucidation of BFA function in Saccharomyces cerevisiae using genetic methods reveals that cell growth is stopped when BFA is added to the Saccharomyces cerevisiae cell strains.

Published
1994

14. Inheritance of the Golgi Apparatus and Cytokinesis Are Controlled by Degradation of GBF1

Author

Magliozzi, Roberto, Carrero, Zunamys I., Low, Teck Yew, Yuniati, Laurensia, Valdes-Quezada, Christian, Kruiswijk, Flore, van Wijk, Koen, Heck, Albert J.R., Jackson, Catherine L., Guardavaccaro, Daniele, Magliozzi, Roberto, Carrero, Zunamys I., Low, Teck Yew, Yuniati, Laurensia, Valdes-Quezada, Christian, Kruiswijk, Flore, van Wijk, Koen, Heck, Albert J.R., Jackson, Catherine L., and Guardavaccaro, Daniele

Published
2018

15. Inheritance of the Golgi Apparatus and Cytokinesis Are Controlled by Degradation of GBF1

Author

Afd Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Biomolecular Mass Spectrometry and Proteomics, Magliozzi, Roberto, Carrero, Zunamys I, Low, Teck Yew, Yuniati, Laurensia, Valdes-Quezada, Christian, Kruiswijk, Flore, van Wijk, Koen, Heck, Albert J R, Jackson, Catherine L, Guardavaccaro, Daniele, Afd Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Biomolecular Mass Spectrometry and Proteomics, Magliozzi, Roberto, Carrero, Zunamys I, Low, Teck Yew, Yuniati, Laurensia, Valdes-Quezada, Christian, Kruiswijk, Flore, van Wijk, Koen, Heck, Albert J R, Jackson, Catherine L, and Guardavaccaro, Daniele

Published
2018

16. Inheritance of the Golgi Apparatus and Cytokinesis Are Controlled by Degradation of GBF1

Author

Hubrecht Institute with UMC, Cancer, Magliozzi, Roberto, Carrero, Zunamys I., Low, Teck Yew, Yuniati, Laurensia, Valdes-Quezada, Christian, Kruiswijk, Flore, van Wijk, Koen, Heck, Albert J.R., Jackson, Catherine L., Guardavaccaro, Daniele, Hubrecht Institute with UMC, Cancer, Magliozzi, Roberto, Carrero, Zunamys I., Low, Teck Yew, Yuniati, Laurensia, Valdes-Quezada, Christian, Kruiswijk, Flore, van Wijk, Koen, Heck, Albert J.R., Jackson, Catherine L., and Guardavaccaro, Daniele

Published
2018

17. Arf Proteins and Their Regulators: At the Interface Between Membrane Lipids and the Protein Trafficking Machinery

Author

Jackson, Catherine L.

Subjects
GTPase activating protein (GAP), ADP ribosylation factor (Arf), lipid trafficking, guanine nucleotide-exchange factor (GEF), membrane, vesicular trafficking, membrane contact site (MCS), lipid kinase, Article, vesicle coat protein
Abstract

The Arf small GTP-binding (G) proteins regulate membrane traffic and organelle structure in eukaryotic cells through a regulated cycle of GTP binding and hydrolysis. The first function identified for Arf proteins was recruitment of cytosolic coat complexes to membranes to mediate vesicle formation. However, subsequent studies have uncovered additional functions, including roles in plasma membrane signalling pathways, cytoskeleton regulation, lipid droplet function, and non-vesicular lipid transport. In contrast to other families of G proteins, there are only a few Arf proteins in each organism, yet they function specifically at many different cellular locations. Part of this specificity is achieved by formation of complexes with their guanine nucleotide-exchange factors (GEFs) and GTPase activating proteins (GAPs) that catalyse GTP binding and hydrolysis, respectively. Because these regulators outnumber their Arf substrates by at least 3-to-1, an important aspect of understanding Arf function is elucidating the mechanisms by which a single Arf protein is incorporated into different GEF, GAP, and effector complexes. New insights into these mechanisms have come from recent studies showing GEF–effector interactions, Arf activation cascades, and positive feedback loops. A unifying theme in the function of Arf proteins, carried out in conjunction with their regulators and effectors, is sensing and modulating the properties of the lipids that make up cellular membranes.

Published
2014

24. Endosome-specific localization and function of the ARF activator GNOM

Author

Bonificino, Juan S. and Jackson, Catherine L.

Subjects
Cell research -- Analysis, Adenosine diphosphate -- Physiological aspects, Lysosomes -- Physiological aspects, Secretion -- Genetic aspects, Secretion -- Physiological aspects, Cell membranes -- Genetic aspects, Cell membranes -- Physiological aspects, Guanosine triphosphatase -- Physiological aspects, Ribosomes -- Genetic aspects, Ribosomes -- Physiological aspects, Gene mutations -- Physiological aspects, Guanine -- Physiological aspects, Nucleotides -- Genetic aspects, Nucleotides -- Physiological aspects, Biological sciences
Abstract

The authors discuss ADP-ribosylation factor proteins. The topics of interest include the involvement of mammalian ADP-ribosylation factor - guanine-nucleotide exchange factors in coat recruitment to endosomes and sorting in polarized cells.

Published
2003

25. Coordinated Polar Localization of Auxin Efflux Carrier PIN1 by GNOM ARF GEF

Author

Steinman, Thomas, Geldner, Niko, Grebe, Markus, Mangold, Stefan, Jackson, Catherine L., Paris, Sonia, Galweiler, Leo, Palme, Klaus, and Jurgens, Gerd

Subjects
Plant hormones -- Research, Developmental genetics -- Research, Auxins -- Research, Science and technology
Abstract

The plant hormone auxin is transported in a polar manner along the shoot-root axis, which requires efflux carriers such as PIN1. Asymmetric localization of PIN1 develops from a random distribution in Arabidopsis early embryogenesis. Coordinated polar localization of PIN1 is defective in gnom embryos. GNON is a membrane-associated guanine-nucleotide exchange factor on ADP-ribosylation factor G protein (ARF GEF). Thus, GNOM-dependent vesicle trafficking may establish cell polarity, resulting in polar auxin transport., Polar auxin transport has been implicated in a variety of developmental processes, including phototropism, gravitropism, apical dominance, root formation, and vascular tissue patterning (1, 2). These vectorial processes require coordinated [...]

Published
1999

28. Identification of GBF1 as a cellular factor required for hepatitis E virus RNA replication.

Author

Farhat, Rayan, Ankavay, Maliki, Lebsir, Nadjet, Gouttenoire, Jérôme, Jackson, Catherine L., Wychowski, Czeslaw, Moradpour, Darius, Dubuisson, Jean, Rouillé, Yves, and Cocquerel, Laurence

Subjects
HEPATITIS E virus, GUANINE nucleotide exchange factors, BREFELDIN, CATALYTIC domains, RNA viruses
Abstract

The hepatitis E virus (HEV) genome is a single-stranded, positive-sense RNA that encodes three proteins including the ORF1 replicase. Mechanisms of HEV replication in host cells are unclear, and only a few cellular factors involved in this step have been identified so far. Here, we used brefeldin A (BFA) that blocks the activity of the cellular Arf guanine nucleotide exchange factors GBF1, BIG1, and BIG2, which play a major role in reshuffling of cellular membranes. We showed that BFA inhibits HEV replication in a dose-dependent manner. The use of siRNA and Golgicide A identified GBF1 as a host factor critically involved in HEV replication. Experiments using cells expressing a mutation in the catalytic domain of GBF1 and overexpression of wild type GBF1 or a BFA-resistant GBF1 mutant rescuing HEV replication in BFA-treated cells, confirmed that GBF1 is the only BFA-sensitive factor required for HEV replication. We demonstrated that GBF1 is likely required for the activity of HEV replication complexes. However, GBF1 does not colocalise with the ORF1 protein, and its subcellular distribution is unmodified upon infection or overexpression of viral proteins, indicating that GBF1 is likely not recruited to replication sites. Together, our results suggest that HEV replication involves GBF1-regulated mechanisms. [ABSTRACT FROM AUTHOR]

Published
2018
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33. Meeting report – Arf and Rab family G proteins

Author

Casanova, James E., primary, Hsu, Victor W., additional, Jackson, Catherine L., additional, Kahn, Richard A., additional, Roy, Craig R., additional, Stow, Jennifer L., additional, Wandinger-Ness, Angela, additional, and Sztul, Elizabeth, additional

Published
2013
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34. Interaction between the triglyceride lipase ATGL and the arf1 activator GBF1

Author

Ellong, Emy Njoh, Soni, Krishnakant G., Bui, Quynh-Trang, Sougrat, Rachid, Golinelli-Cohen, Marie-Pierre, Jackson, Catherine L., Ellong, Emy Njoh, Soni, Krishnakant G., Bui, Quynh-Trang, Sougrat, Rachid, Golinelli-Cohen, Marie-Pierre, and Jackson, Catherine L.

Abstract

The Arf1 exchange factor GBF1 (Golgi Brefeldin A resistance factor 1) and its effector COPI are required for delivery of ATGL (adipose triglyceride lipase) to lipid droplets (LDs). Using yeast two hybrid, co-immunoprecipitation in mammalian cells and direct protein binding approaches, we report here that GBF1 and ATGL interact directly and in cells, through multiple contact sites on each protein. The C-terminal region of ATGL interacts with N-terminal domains of GBF1, including the catalytic Sec7 domain, but not with full-length GBF1 or its entire N-terminus. The N-terminal lipase domain of ATGL (called the patatin domain) interacts with two C-terminal domains of GBF1, HDS (Homology downstream of Sec7) 1 and HDS2. These two domains of GBF1 localize to lipid droplets when expressed alone in cells, but not to the Golgi, unlike the full-length GBF1 protein, which localizes to both. We suggest that interaction of GBF1 with ATGL may be involved in the membrane trafficking pathway mediated by GBF1, Arf1 and COPI that contributes to the localization of ATGL to lipid droplets.

Published
2011

48. Interactions between Conserved Domains within Homodimers in the BIG1, BIG2, and GBF1 Arf Guanine Nucleotide Exchange Factors

Author

Ramaen, Odile, primary, Joubert, Alexandra, additional, Simister, Philip, additional, Belgareh-Touzé, Naïma, additional, Olivares-Sanchez, Maria Conception, additional, Zeeh, Jean-Christophe, additional, Chantalat, Sophie, additional, Golinelli-Cohen, Marie-Pierre, additional, Jackson, Catherine L., additional, Biou, Valérie, additional, and Cherfils, Jacqueline, additional

Published
2007
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