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Journal articles
The autophagy protein ATG16L1 cooperates with IFT20 and INPP5E to regulate the turnover of phosphoinositides at the primary cilium
Abstract : The primary cilium (PC) regulates signalization linked to external stress sensing. Previous works established a functional interplay between the PC and the autophagic machinery. When ciliogenesis is promoted by serum deprivation, the autophagy protein ATG16L1 and the ciliary protein IFT20 are co-transported to the PC. Here, we demonstrate that IFT20 and ATG16L1 are part of the same complex requiring the WD40 domain of ATG16L1 and a Y-E-F-I motif in IFT20. We show that ATG16L1-deficient cells exhibit aberrant ciliary structures, which accumulate PI4,5P2, whereas PI4P, a lipid normally concentrated in the PC, is absent. Finally, we demonstrate that INPP5E, a phosphoinositide-associated phosphatase responsible for PI4P generation, interacts with ATG16L1 and that a perturbation of the ATG16L1/IFT20 complex alters its trafficking to the PC. Altogether, our results reveal a function of ATG16L1 in ciliary lipid and protein trafficking, thus directly contributing to proper PC dynamics and functions.
https://hal-univ-paris.archives-ouvertes.fr/hal-03246943
Contributor : Equipe Hal Université de Paris Connect in order to contact the contributor
Submitted on : Wednesday, June 2, 2021 - 4:41:30 PM
Last modification on : Tuesday, September 28, 2021 - 5:13:18 PM
Long-term archiving on: : Friday, September 3, 2021 - 7:51:08 PM
Contributor : Equipe Hal Université de Paris Connect in order to contact the contributor
Submitted on : Wednesday, June 2, 2021 - 4:41:30 PM
Last modification on : Tuesday, September 28, 2021 - 5:13:18 PM
Long-term archiving on: : Friday, September 3, 2021 - 7:51:08 PM
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