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Thursday 6 of May, 2021
The key autophagic protein ATG16L1 contributes to primary cilium membrane trafficking

A study conducted in the Morel laboratory and recently published in Cell Reports highlights the role of autophagic protein ATG16L1 in the context of ciliogenesis, in response to nutritional stress. These data describe a non-canonical function of ATG16L1, which participates to post-Golgi trafficking of key ciliary IFT20 protein, via a direct interaction mediated by its WD40 domain and a novel ATG16L1-binding motif present in IFT20. The ATG16L1-IFT20 complex regulates the phosphoinositides turnover required at primary cilium membrane by targeting the PI4,5P2-associated INPP5E phosphatase to the site of ciliogenesis, enabling local synthesis of PI4P, a key marker of primary cilium membrane identity. Importantly, these findings demonstrate that ATG16L1 is mobilized in the ciliogenesis process independently of autophagy, by acting as a local regulator of phosphoinositides equilibrium at plasma membrane.

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