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Septin6 and Septin7 GTP binding proteins regulate AP-3- and ESCRT-dependent multivesicular body biogenesis.
Traikov, Sofia; Stange, Christoph; Wassmer, Thomas; Paul-Gilloteaux, Perrine; Salamero, Jean; Raposo, Graça; Hoflack, Bernard.
Afiliación
  • Traikov S; Biotechnological Center, Technische Universität Dresden, Dresden, Germany.
  • Stange C; Biotechnological Center, Technische Universität Dresden, Dresden, Germany.
  • Wassmer T; Biotechnological Center, Technische Universität Dresden, Dresden, Germany; School of Life and Health Sciences, Aston University, Birmingham, United Kingdom.
  • Paul-Gilloteaux P; Molecular Mechanisms of Intracellular Transport Laboratory, CNRS-Institut Curie, Paris, France; Cell and Tissue Imaging Facility, PICT-IBiSA & Nikon Imaging Center, CNRS-Institut Curie, Paris, France.
  • Salamero J; Molecular Mechanisms of Intracellular Transport Laboratory, CNRS-Institut Curie, Paris, France; Cell and Tissue Imaging Facility, PICT-IBiSA & Nikon Imaging Center, CNRS-Institut Curie, Paris, France.
  • Raposo G; Molecular Mechanisms of Intracellular Transport Laboratory, CNRS-Institut Curie, Paris, France.
  • Hoflack B; Biotechnological Center, Technische Universität Dresden, Dresden, Germany.
PLoS One ; 9(11): e109372, 2014.
Article en En | MEDLINE | ID: mdl-25380047
Septins (SEPTs) form a family of GTP-binding proteins implicated in cytoskeleton and membrane organization, cell division and host/pathogen interactions. The precise function of many family members remains elusive. We show that SEPT6 and SEPT7 complexes bound to F-actin regulate protein sorting during multivesicular body (MVB) biogenesis. These complexes bind AP-3, an adapter complex sorting cargos destined to remain in outer membranes of maturing endosomes, modulate AP-3 membrane interactions and the motility of AP-3-positive endosomes. These SEPT-AP interactions also influence the membrane interaction of ESCRT (endosomal-sorting complex required for transport)-I, which selects ubiquitinated cargos for degradation inside MVBs. Whereas our findings demonstrate that SEPT6 and SEPT7 function in the spatial, temporal organization of AP-3- and ESCRT-coated membrane domains, they uncover an unsuspected coordination of these sorting machineries during MVB biogenesis. This requires the E3 ubiquitin ligase LRSAM1, an AP-3 interactor regulating ESCRT-I sorting activity and whose mutations are linked with Charcot-Marie-Tooth neuropathies.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Ciclo Celular / Complejo 3 de Proteína Adaptadora / Cuerpos Multivesiculares / Complejos de Clasificación Endosomal Requeridos para el Transporte / Septinas Límite: Humans Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2014 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Ciclo Celular / Complejo 3 de Proteína Adaptadora / Cuerpos Multivesiculares / Complejos de Clasificación Endosomal Requeridos para el Transporte / Septinas Límite: Humans Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2014 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos