ER–plasma membrane contact sites contribute to autophagosome biogenesis by regulation of local PI3P synthesis

• Published in: The EMBO journal Vol. 36; no. 14; pp. 2018 - 2033
• Main Authors: Nascimbeni, Anna Chiara, Giordano, Francesca, Dupont, Nicolas, Grasso, Daniel, Vaccaro, Maria I, Codogno, Patrice, Morel, Etienne
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 14.07.2017; Springer Nature B.V; EMBO Press; John Wiley and Sons Inc
• Subjects: Animals; autophagosome; Autophagosomes - metabolism; Autophagy; Biosynthesis; Carrier Proteins - metabolism; Cell Membrane - metabolism; Cellular Biology; contact sites; Cortex; Dogs; EMBO07; EMBO20; Endoplasmic reticulum; Endoplasmic Reticulum - metabolism; extended synaptotagmins; HeLa Cells; Humans; Life Sciences; Madin Darby Canine Kidney Cells; Markers; Membrane proteins; Membrane Proteins - metabolism; Membranes; Organelle Biogenesis; Phagocytosis; Phosphate; Phosphatidylinositol Phosphates - metabolism; PI3P; Plasma; Proteins; Recruitment; Synaptotagmins - metabolism; Synthesis; Tethering; Tethers; contact sites; organelle biogenesis; extended synaptotagmins; PI3P; autophagosome; PI3P Subject Categories Autophagy & Cell Death; Membrane & Intracellular

The double‐membrane‐bound autophagosome is formed by the closure of a structure called the phagophore, origin of which is still unclear. The endoplasmic reticulum (ER) is clearly implicated in autophagosome biogenesis due to the presence of the omegasome subdomain positive for DFCP1, a phosphatidyl‐...