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Septin 9 has Two Polybasic Domains Critical to Septin Filament Assembly and Golgi Integrity.
Omrane, Mohyeddine; Camara, Amanda Souza; Taveneau, Cyntia; Benzoubir, Nassima; Tubiana, Thibault; Yu, Jinchao; Guérois, Raphaël; Samuel, Didier; Goud, Bruno; Poüs, Christian; Bressanelli, Stéphane; Garratt, Richard Charles; Thiam, Abdou Rachid; Gassama-Diagne, Ama.
Afiliación
  • Omrane M; INSERM, Unité 1193, Villejuif 94800, France; Université Paris-Sud, UMR-S 1193, Villejuif 94800, France; Laboratoire de Physique de l'Ecole Normale Supérieure, ENS, Université PSL, CNRS, Sorbonne Université, Université Paris-Diderot, Sorbonne Paris Cité, Paris, France.
  • Camara AS; Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, Brazil.
  • Taveneau C; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif Sur Yvette Cedex, France.
  • Benzoubir N; INSERM, Unité 1193, Villejuif 94800, France; Université Paris-Sud, UMR-S 1193, Villejuif 94800, France.
  • Tubiana T; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif Sur Yvette Cedex, France.
  • Yu J; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif Sur Yvette Cedex, France; Commissariat à l'Energie Atomique et aux Energies Alternatives, 91191 Gif-Sur- Yvette Cedex, France.
  • Guérois R; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif Sur Yvette Cedex, France; Commissariat à l'Energie Atomique et aux Energies Alternatives, 91191 Gif-Sur- Yvette Cedex, France.
  • Samuel D; INSERM, Unité 1193, Villejuif 94800, France; Université Paris-Sud, UMR-S 1193, Villejuif 94800, France.
  • Goud B; Institute Curie, PSL Research University, CNRS UMR 144, Paris, France.
  • Poüs C; INSERM, Unité 1193, Villejuif 94800, France; Université Paris-Sud, UMR-S 1193, Villejuif 94800, France.
  • Bressanelli S; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif Sur Yvette Cedex, France.
  • Garratt RC; Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, Brazil.
  • Thiam AR; Laboratoire de Physique de l'Ecole Normale Supérieure, ENS, Université PSL, CNRS, Sorbonne Université, Université Paris-Diderot, Sorbonne Paris Cité, Paris, France. Electronic address: thiam@ens.fr.
  • Gassama-Diagne A; INSERM, Unité 1193, Villejuif 94800, France; Université Paris-Sud, UMR-S 1193, Villejuif 94800, France. Electronic address: ama.gassama@inserm.fr.
iScience ; 13: 138-153, 2019 Mar 29.
Article en En | MEDLINE | ID: mdl-30831549
Septins are GTP-binding proteins involved in several membrane remodeling mechanisms. They associate with membranes, presumably using a polybasic domain (PB1) that interacts with phosphoinositides (PIs). Membrane-bound septins assemble into microscopic structures that regulate membrane shape. How septins interact with PIs and then assemble and shape membranes is poorly understood. Here, we found that septin 9 has a second polybasic domain (PB2) conserved in the human septin family. Similar to PB1, PB2 binds specifically to PIs, and both domains are critical for septin filament formation. However, septin 9 membrane association is not dependent on these PB domains, but on putative PB-adjacent amphipathic helices. The presence of PB domains guarantees protein enrichment in PI-contained membranes, which is critical for PI-enriched organelles. In particular, we found that septin 9 PB domains control the assembly and functionality of the Golgi apparatus. Our findings offer further insight into the role of septins in organelle morphology.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: IScience Año: 2019 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: IScience Año: 2019 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Estados Unidos