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Role of the Sec22b-E-Syt complex in neurite growth and ramification.
Gallo, Alessandra; Danglot, Lydia; Giordano, Francesca; Hewlett, Bailey; Binz, Thomas; Vannier, Christian; Galli, Thierry.
Afiliación
  • Gallo A; Université de Paris, Institute of Psychiatry and Neuroscience of Paris (IPNP), INSERM, Membrane Traffic in Healthy & Diseased Brain, F-75014 Paris, France.
  • Danglot L; Ecole des Neurosciences de Paris (ENP), F-75006 Paris, France.
  • Giordano F; Université de Paris, Institute of Psychiatry and Neuroscience of Paris (IPNP), INSERM, Membrane Traffic in Healthy & Diseased Brain, F-75014 Paris, France.
  • Hewlett B; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Paris-Sud University, Paris-Saclay University, Gif-sur-Yvette cedex, 91198, France.
  • Binz T; Université de Paris, Institute of Psychiatry and Neuroscience of Paris (IPNP), INSERM, Membrane Traffic in Healthy & Diseased Brain, F-75014 Paris, France.
  • Vannier C; Medizinische Hochschule Hannover, Institut für Physiologische Chemie OE4310, 30625 Hannover, Germany.
  • Galli T; Université de Paris, Institute of Psychiatry and Neuroscience of Paris (IPNP), INSERM, Membrane Traffic in Healthy & Diseased Brain, F-75014 Paris, France.
J Cell Sci ; 133(18)2020 09 15.
Article en En | MEDLINE | ID: mdl-32843578
Axons and dendrites are long and often ramified neurites that need particularly intense plasma membrane (PM) expansion during the development of the nervous system. Neurite growth depends on non-fusogenic Sec22b-Stx1 SNARE complexes at endoplasmic reticulum (ER)-PM contacts. Here, we show that Sec22b interacts with members of the extended synaptotagmin (E-Syt) family of ER lipid transfer proteins (LTPs), and this interaction depends on the longin domain of Sec22b. Overexpression of E-Syts stabilizes Sec22b-Stx1 association, whereas silencing of E-Syts has the opposite effect. Overexpression of wild-type E-Syt2, but not mutants unable to transfer lipids or attach to the ER, increase the formation of axonal filopodia and ramification of neurites in developing neurons. This effect is inhibited by a clostridial neurotoxin cleaving Stx1, and expression of the Sec22b longin domain and a Sec22b mutant with an extended linker between the SNARE and transmembrane domains. We conclude that Sec22b-Stx1 ER-PM contact sites contribute to PM expansion by interacting with LTPs, such as E-Syts.This article has an associated First Person interview with the first author of the paper.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neuritas / Retículo Endoplásmico Límite: Humans Idioma: En Revista: J Cell Sci Año: 2020 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido
Texto completo
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Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neuritas / Retículo Endoplásmico Límite: Humans Idioma: En Revista: J Cell Sci Año: 2020 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido