ARF6 Controls Post-Endocytic Recycling through Its Downstream Exocyst Complex Effector

The small guanosine triphosphate (GTP)-binding protein ADP-ribosylation factor (ARF) 6 regulates membrane recycling to regions of plasma membrane remodeling via the endocytic pathway. Here, we show that GTP-bound ARF6 interacts with Sec10, a subunit of the exocyst complex involved in docking of vesi...

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Published inThe Journal of cell biology Vol. 163; no. 5; pp. 1111 - 1121
Main Authors Prigent, Magali, Dubois, Thierry, Raposo, Graça, Derrien, Valérie, Tenza, Danièle, Rossé, Carine, Camonis, Jacques, Chavrier, Philippe
Format Journal Article
LanguageEnglish
Published United States Rockefeller University Press 08.12.2003
The Rockefeller University Press
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Abstract The small guanosine triphosphate (GTP)-binding protein ADP-ribosylation factor (ARF) 6 regulates membrane recycling to regions of plasma membrane remodeling via the endocytic pathway. Here, we show that GTP-bound ARF6 interacts with Sec10, a subunit of the exocyst complex involved in docking of vesicles with the plasma membrane. We found that Sec10 localization in the perinuclear region is not restricted to the trans-Golgi network, but extends to recycling endosomes. In addition, we report that depletion of Sec5 exocyst subunit or dominant inhibition of Sec10 affects the function and the morphology of the recycling pathway. Sec10 is found to redistribute to ruffling areas of the plasma membrane in cells expressing GTP-ARF6, whereas dominant inhibition of Sec10 interferes with ARF6-induced cell spreading. Our paper suggests that ARF6 specifies delivery and insertion of recycling membranes to regions of dynamic reorganization of the plasma membrane through interaction with the vesicle-tethering exocyst complex.
AbstractList The small guanosine triphosphate (GTP)-binding protein ADP-ribosylation factor (ARF) 6 regulates membrane recycling to regions of plasma membrane remodeling via the endocytic pathway. Here, we show that GTP-bound ARF6 interacts with Sec10, a subunit of the exocyst complex involved in docking of vesicles with the plasma membrane. We found that Sec10 localization in the perinuclear region is not restricted to the trans-Golgi network, but extends to recycling endosomes. In addition, we report that depletion of Sec5 exocyst subunit or dominant inhibition of Sec10 affects the function and the morphology of the recycling pathway. Sec10 is found to redistribute to ruffling areas of the plasma membrane in cells expressing GTP-ARF6, whereas dominant inhibition of Sec10 interferes with ARF6-induced cell spreading. Our paper suggests that ARF6 specifies delivery and insertion of recycling membranes to regions of dynamic reorganization of the plasma membrane through interaction with the vesicle-tethering exocyst complex.
The small guanosine triphosphate (GTP)–binding protein ADP-ribosylation factor (ARF) 6 regulates membrane recycling to regions of plasma membrane remodeling via the endocytic pathway. Here, we show that GTP–bound ARF6 interacts with Sec10, a subunit of the exocyst complex involved in docking of vesicles with the plasma membrane. We found that Sec10 localization in the perinuclear region is not restricted to the trans -Golgi network, but extends to recycling endosomes. In addition, we report that depletion of Sec5 exocyst subunit or dominant inhibition of Sec10 affects the function and the morphology of the recycling pathway. Sec10 is found to redistribute to ruffling areas of the plasma membrane in cells expressing GTP-ARF6, whereas dominant inhibition of Sec10 interferes with ARF6-induced cell spreading. Our paper suggests that ARF6 specifies delivery and insertion of recycling membranes to regions of dynamic reorganization of the plasma membrane through interaction with the vesicle-tethering exocyst complex.
The small guanosine triphosphate (GTP)-binding protein ADP-ribosylation factor (ARF) 6 regulates membrane recycling to regions of plasma membrane remodeling via the endocytic pathway. Here, we show that GTP-bound ARF6 interacts with Sec10, a subunit of the exocyst complex involved in docking of vesicles with the plasma membrane. We found that Sec10 localization in the perinuclear region is not restricted to the trans-Golgi network, but extends to recycling endosomes. In addition, we report that depletion of Sec5 exocyst subunit or dominant inhibition of Sec10 affects the function and the morphology of the recycling pathway. Sec10 is found to redistribute to ruffling areas of the plasma membrane in cells expressing GTP-ARF6, whereas dominant inhibition of Sec10 interferes with ARF6-induced cell spreading. Our paper suggests that ARF6 specifies delivery and insertion of recycling membranes to regions of dynamic reorganization of the plasma membrane through interaction with the vesicle-tethering exocyst complex. [PERIODICAL ABSTRACT]
Author Camonis, Jacques
Rossé, Carine
Chavrier, Philippe
Tenza, Danièle
Prigent, Magali
Derrien, Valérie
Raposo, Graça
Dubois, Thierry
AuthorAffiliation 1 Membrane and Cytoskeleton Dynamics Group, Centre National de la Recherche Scientifique, UMR-144
2 Electron Microscopy Laboratory, Centre National de la Recherche Scientifique, UMR-144
3 Institut National de la Santé et de la Recherche Médicale, U-528, Institut Curie, F-75248 Paris Cedex 05, France
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Abbreviations used in this paper: ARF, ADP-ribosylation factor; NRK, normal rat kidney; RE, recycling endosome; siRNA, small interfering RNA; Tf, transferrin; TfR, transferrin-receptor.
The online version of this article contains supplemental material.
Address correspondence to Philippe Chavrier, UMR144 Centre National de la Recherche Scientifique, Institut Curie, 26 rue d'Ulm, F-75248 Paris cedex 05, France. Tel.: 33-1-42-34-63-59. Fax: 33-1-42-34-63-77. email: philippe.chavrier@curie.fr
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PublicationDateYYYYMMDD 2003-12-08
PublicationDate_xml – month: 12
  year: 2003
  text: 20031208
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PublicationDecade 2000
PublicationPlace United States
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PublicationTitle The Journal of cell biology
PublicationTitleAlternate J Cell Biol
PublicationYear 2003
Publisher Rockefeller University Press
The Rockefeller University Press
Publisher_xml – name: Rockefeller University Press
– name: The Rockefeller University Press
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SSID ssj0004743
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Snippet The small guanosine triphosphate (GTP)-binding protein ADP-ribosylation factor (ARF) 6 regulates membrane recycling to regions of plasma membrane remodeling...
The small guanosine triphosphate (GTP)–binding protein ADP-ribosylation factor (ARF) 6 regulates membrane recycling to regions of plasma membrane remodeling...
SourceID pubmedcentral
proquest
crossref
pubmed
jstor
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 1111
SubjectTerms ADP-Ribosylation Factors - genetics
ADP-Ribosylation Factors - metabolism
Animals
Antibodies
B lymphocytes
Cell Line
Cell Membrane - metabolism
Cell membranes
Cell Nucleus - metabolism
Cells
Cellular biology
Cellular immunity
Cytoplasmic Vesicles - metabolism
Endocytosis - physiology
Endosomes - metabolism
Endosomes - ultrastructure
Epithelial cells
Fungal Proteins - genetics
Fungal Proteins - metabolism
Guanosine Triphosphate - metabolism
HeLa cells
Humans
Membranes
P branes
Plasma
Plasma interactions
Protein Transport
Recombinant Fusion Proteins - metabolism
Recycling
RNA, Small Interfering - metabolism
Saccharomyces cerevisiae Proteins
trans-Golgi Network - metabolism
trans-Golgi Network - ultrastructure
Transferrin - metabolism
Two-Hybrid System Techniques
Vesicular Transport Proteins
Title ARF6 Controls Post-Endocytic Recycling through Its Downstream Exocyst Complex Effector
URI https://www.jstor.org/stable/1621922
https://www.ncbi.nlm.nih.gov/pubmed/14662749
https://www.proquest.com/docview/217083404/abstract/
https://search.proquest.com/docview/71442098
https://pubmed.ncbi.nlm.nih.gov/PMC2173613
Volume 163
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