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When the autophagy protein ATG16L1 met the ciliary protein IFT20.
Boukhalfa, Asma; Roccio, Federica; Dupont, Nicolas; Codogno, Patrice; Morel, Etienne.
Afiliación
  • Boukhalfa A; Institut Necker-Enfants Malades (INEM), Université de Paris, Paris, France.
  • Roccio F; Institut Necker-Enfants Malades (INEM), Université de Paris, Paris, France.
  • Dupont N; Institut Necker-Enfants Malades (INEM), Université de Paris, Paris, France.
  • Codogno P; Institut Necker-Enfants Malades (INEM), Université de Paris, Paris, France.
  • Morel E; Institut Necker-Enfants Malades (INEM), Université de Paris, Paris, France.
Autophagy ; 17(7): 1791-1793, 2021 07.
Article en En | MEDLINE | ID: mdl-34057021
ABSTRACT
The primary cilium (PC), a plasma membrane microtubule-based structure, is a sensor of extracellular chemical and mechanical stress stimuli. Upon ciliogenesis, the autophagy protein ATG16L1 and the ciliary protein IFT20 are co-transported to the PC. We demonstrated in a recent study that IFT20 and ATG16L1 interact in a multiprotein complex. This interaction is mediated by the ATG16L1 WD40 domain and an ATG16L1-binding motif newly identified in IFT20. ATG16L1-deficient cells are decorated by giant ciliary structures hallmarked by defects in PC-associated signaling. These structures uncommonly accumulate phosphatidylinositol-4,5-bisphosphate (PtdIns[4,5]P2) while phosphatidylinositol-4-phosphate (PtdIns4P), a lipid normally concentrated in the PC, is excluded. We show that INPP5E, a phosphoinositide-associated phosphatase responsible for PtdIns4P generation, is a partner of ATG16L1 in this context. Perturbation of the ATG16L1-IFT20 complex alters INPP5E trafficking and proper function at the ciliary membrane. Altogether, these results reveal a novel autophagy-independent function of ATG16L1 that contributes to proper PC dynamics and function.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Autofagia / Monoéster Fosfórico Hidrolasas Idioma: En Revista: Autophagy Año: 2021 Tipo del documento: Article País de afiliación: Francia

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Autofagia / Monoéster Fosfórico Hidrolasas Idioma: En Revista: Autophagy Año: 2021 Tipo del documento: Article País de afiliación: Francia