Ral GTPases Regulate Exocyst Assembly through Dual Subunit Interactions
Ral GTPases have been implicated in the regulation of a variety of dynamic cellular processes including proliferation, oncogenic transformation, actin-cytoskeletal dynamics, endocytosis, and exocytosis. Recently the Sec6/8 complex, or exocyst, a multisubunit complex facilitating post-Golgi targeting...
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Published in | The Journal of biological chemistry Vol. 278; no. 51; pp. 51743 - 51748 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
19.12.2003
American Society for Biochemistry and Molecular Biology |
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Abstract | Ral GTPases have been implicated in the regulation of a variety of dynamic cellular processes including proliferation, oncogenic transformation, actin-cytoskeletal dynamics, endocytosis, and exocytosis. Recently the Sec6/8 complex, or exocyst, a multisubunit complex facilitating post-Golgi targeting of distinct subclasses of secretory vesicles, has been identified as a bona fide Ral effector complex. Ral GTPases regulate exocyst-dependent vesicle trafficking and are required for exocyst complex assembly. Sec5, a membrane-associated exocyst subunit, has been identified as a direct target of activated Ral; however, the mechanism by which Ral can modulate exocyst assembly is unknown. Here we report that an additional component of the exocyst, Exo84, is a direct target of activated Ral. We provide evidence that mammalian exocyst components are present as distinct subcomplexes on vesicles and the plasma membrane and that Ral GTPases regulate the assembly interface of a full octameric exocyst complex through interaction with Sec5 and Exo84. |
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AbstractList | Ral GTPases have been implicated in the regulation of a variety of dynamic cellular processes including proliferation, oncogenic transformation, actin-cytoskeletal dynamics, endocytosis, and exocytosis. Recently the Sec6/8 complex, or exocyst, a multisubunit complex facilitating post-Golgi targeting of distinct subclasses of secretory vesicles, has been identified as a bona fide Ral effector complex. Ral GTPases regulate exocyst-dependent vesicle trafficking and are required for exocyst complex assembly. Sec5, a membrane-associated exocyst subunit, has been identified as a direct target of activated Ral; however, the mechanism by which Ral can modulate exocyst assembly is unknown. Here we report that an additional component of the exocyst, Exo84, is a direct target of activated Ral. We provide evidence that mammalian exocyst components are present as distinct subcomplexes on vesicles and the plasma membrane and that Ral GTPases regulate the assembly interface of a full octameric exocyst complex through interaction with Sec5 and Exo84. Ral GTPases have been implicated in the regulation of a variety of dynamic cellular processes including proliferation, oncogenic transformation, actin-cytoskeletal dynamics, endocytosis, and exocytosis. Recently the Sec6/8 complex, or exocyst, a multisubunit complex facilitating post-Golgi targeting of distinct subclasses of secretory vesicles, has been identified as a bona fide Ral effector complex. Ral GTPases regulate exocyst-dependent vesicle trafficking and are required for exocyst complex assembly. Sec5, a membrane-associated exocyst subunit, has been identified as a direct target of activated Ral; however, the mechanism by which Ral can modulate exocyst assembly is unknown. Here we report that an additional component of the exocyst, Exo84, is a direct target of activated Ral. We provide evidence that mammalian exocyst components are present as distinct subcomplexes on vesicles and the plasma membrane and that Ral GTPases regulate the assembly interface of a full octameric exocyst complex through interaction with Sec5 and Exo84. |
Author | Formstecher, Etienne Camonis, Jacques Mirey, Gladys Daviet, Laurent White, Michael A. Tong, Chao Rosse, Carine Moskalenko, Serge |
Author_xml | – sequence: 1 givenname: Serge surname: Moskalenko fullname: Moskalenko, Serge organization: Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9039 – sequence: 2 givenname: Chao surname: Tong fullname: Tong, Chao organization: Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9039 – sequence: 3 givenname: Carine surname: Rosse fullname: Rosse, Carine organization: Hybrigenics, 3-5 impasse Reille, 75014 Paris, France – sequence: 4 givenname: Gladys surname: Mirey fullname: Mirey, Gladys organization: Hybrigenics, 3-5 impasse Reille, 75014 Paris, France – sequence: 5 givenname: Etienne surname: Formstecher fullname: Formstecher, Etienne organization: Hybrigenics, 3-5 impasse Reille, 75014 Paris, France – sequence: 6 givenname: Laurent surname: Daviet fullname: Daviet, Laurent organization: Hybrigenics, 3-5 impasse Reille, 75014 Paris, France – sequence: 7 givenname: Jacques surname: Camonis fullname: Camonis, Jacques organization: Institute Curie, Paris, France – sequence: 8 givenname: Michael A. surname: White fullname: White, Michael A. email: Michael.white@UTSouthwestern.edu organization: Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9039 |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/14525976$$D View this record in MEDLINE/PubMed https://hal.inrae.fr/hal-02679145$$DView record in HAL |
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Snippet | Ral GTPases have been implicated in the regulation of a variety of dynamic cellular processes including proliferation, oncogenic transformation,... Ral GTPases have been implicated in the regulation of a variety of dynamic cellular processes including proliferation, oncogenic transformation,... |
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SubjectTerms | Carrier Proteins - metabolism Cell Line Humans Life Sciences Macromolecular Substances Membrane Proteins - metabolism Other Protein Binding Protein Subunits - metabolism ral GTP-Binding Proteins - metabolism ral GTP-Binding Proteins - physiology Secretory Vesicles - metabolism Transfection Vesicular Transport Proteins |
Title | Ral GTPases Regulate Exocyst Assembly through Dual Subunit Interactions |
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