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 in | The Journal of cell biology Vol. 163; no. 5; pp. 1111 - 1121 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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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. |
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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 |
AuthorAffiliation_xml | – name: 2 Electron Microscopy Laboratory, Centre National de la Recherche Scientifique, UMR-144 – name: 1 Membrane and Cytoskeleton Dynamics Group, Centre National de la Recherche Scientifique, UMR-144 – name: 3 Institut National de la Santé et de la Recherche Médicale, U-528, Institut Curie, F-75248 Paris Cedex 05, France |
Author_xml | – sequence: 1 givenname: Magali surname: Prigent fullname: Prigent, Magali – sequence: 2 givenname: Thierry surname: Dubois fullname: Dubois, Thierry – sequence: 3 givenname: Graça surname: Raposo fullname: Raposo, Graça – sequence: 4 givenname: Valérie surname: Derrien fullname: Derrien, Valérie – sequence: 5 givenname: Danièle surname: Tenza fullname: Tenza, Danièle – sequence: 6 givenname: Carine surname: Rossé fullname: Rossé, Carine – sequence: 7 givenname: Jacques surname: Camonis fullname: Camonis, Jacques – sequence: 8 givenname: Philippe surname: Chavrier fullname: Chavrier, Philippe |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/14662749$$D View this record in MEDLINE/PubMed |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 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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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... |
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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 |
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