Interaction between the triglyceride lipase ATGL and the arf1 activator GBF1

Handle URI:
http://hdl.handle.net/10754/325290
Title:
Interaction between the triglyceride lipase ATGL and the arf1 activator GBF1
Authors:
Ellong, Emy Njoh; Soni, Krishnakant G.; Bui, Quynh-Trang; Sougrat, Rachid; Golinelli-Cohen, Marie-Pierre; 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.
KAUST Department:
Advanced Nanofabrication, Imaging and Characterization Core Lab
Citation:
Ellong EN, Soni KG, Bui Q-T, Sougrat R, Golinelli-Cohen M-P, et al. (2011) Interaction between the Triglyceride Lipase ATGL and the Arf1 Activator GBF1. PLoS ONE 6: e21889. doi:10.1371/journal.pone.0021889.
Publisher:
Public Library of Science (PLoS)
Journal:
PLoS ONE
Issue Date:
18-Jul-2011
DOI:
10.1371/journal.pone.0021889
PubMed ID:
21789191
PubMed Central ID:
PMC3138737
Type:
Article
ISSN:
19326203
Appears in Collections:
Articles; Advanced Nanofabrication, Imaging and Characterization Core Lab

Full metadata record

DC FieldValue Language
dc.contributor.authorEllong, Emy Njohen
dc.contributor.authorSoni, Krishnakant G.en
dc.contributor.authorBui, Quynh-Trangen
dc.contributor.authorSougrat, Rachiden
dc.contributor.authorGolinelli-Cohen, Marie-Pierreen
dc.contributor.authorJackson, Catherine L.en
dc.date.accessioned2014-08-27T09:45:12Z-
dc.date.available2014-08-27T09:45:12Z-
dc.date.issued2011-07-18en
dc.identifier.citationEllong EN, Soni KG, Bui Q-T, Sougrat R, Golinelli-Cohen M-P, et al. (2011) Interaction between the Triglyceride Lipase ATGL and the Arf1 Activator GBF1. PLoS ONE 6: e21889. doi:10.1371/journal.pone.0021889.en
dc.identifier.issn19326203en
dc.identifier.pmid21789191en
dc.identifier.doi10.1371/journal.pone.0021889en
dc.identifier.urihttp://hdl.handle.net/10754/325290en
dc.description.abstractThe 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.en
dc.language.isoenen
dc.publisherPublic Library of Science (PLoS)en
dc.rightsThis is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication.en
dc.rightsArchived with thanks to PLoS ONEen
dc.subjectadenosine diphosphate ribosylation factor 1en
dc.subjectadipose triglyceride lipaseen
dc.subjectcell proteinen
dc.subjectcoat protein complex Ien
dc.subjectfat dropleten
dc.subjectGolgi Brefeldin A resistance factor 1 proteinen
dc.subjectguanine nucleotide exchange factoren
dc.subjecttriacylglycerol lipaseen
dc.subjectunclassified drugen
dc.subjectadenosine diphosphate ribosylation factor 1en
dc.subjectGBF1 protein, humanen
dc.subjectguanine nucleotide exchange factoren
dc.subjectlipiden
dc.subjectPNPLA2 protein, humanen
dc.subjecttriacylglycerol lipaseen
dc.subjectamino terminal sequenceen
dc.subjectcarboxy terminal sequenceen
dc.subjectcontrolled studyen
dc.subjectenzyme activityen
dc.subjectGolgi complexen
dc.subjectintracellular transporten
dc.subjectmembrane transporten
dc.subjectprotein domainen
dc.subjectprotein expressionen
dc.subjectprotein localizationen
dc.subjectprotein protein interactionen
dc.subjectsignal transductionen
dc.subjectbiocatalysisen
dc.subjectchemistryen
dc.subjectHeLa cellen
dc.subjectimmunoelectron microscopyen
dc.subjectimmunoprecipitationen
dc.subjectmetabolismen
dc.subjectprotein analysisen
dc.subjectprotein bindingen
dc.subjectprotein tertiary structureen
dc.subjectprotein transporten
dc.subjecttwo hybrid systemen
dc.subjectMammaliaen
dc.subjectADP-Ribosylation Factor 1en
dc.subjectBiocatalysisen
dc.subjectGuanine Nucleotide Exchange Factorsen
dc.subjectHeLa Cellsen
dc.subjectImmunoprecipitationen
dc.subjectLipaseen
dc.subjectLipidsen
dc.subjectMicroscopy, Immunoelectronen
dc.subjectProtein Bindingen
dc.subjectProtein Interaction Mappingen
dc.subjectProtein Structure, Tertiaryen
dc.subjectProtein Transporten
dc.subjectTwo-Hybrid System Techniquesen
dc.titleInteraction between the triglyceride lipase ATGL and the arf1 activator GBF1en
dc.typeArticleen
dc.contributor.departmentAdvanced Nanofabrication, Imaging and Characterization Core Laben
dc.identifier.journalPLoS ONEen
dc.identifier.pmcidPMC3138737en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionLaboratoire d'Enzymologie et Biochimie Structurales, Bat 34, Centre National de la Recherche Scientifique (CNRS), Gif-sur-Yvette, Franceen
dc.contributor.institutionCell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, United Statesen
dc.contributor.institutionLaboratoire de Biologie Cellulaire, Institut Jean-Pierre Bourgin, Institut National de la Recherche Agronomique (INRA), Versailles, Franceen
dc.contributor.institutionInstitut Jacques Monod, CNRS and Universit Paris Diderot-Paris 7, Paris, Franceen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorSougrat, Rachiden

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