WIPI2B links PtdIns3P to LC3 lipidation through binding ATG16L1 |
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| Authors: | Hannah C Dooley Michael I Wilson Sharon A Tooze |
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| Affiliation: | 1.London Research Institute; Cancer Research UK; London, UK;2.The Babraham Institute; Babraham Research Campus; Cambridge, UK |
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| Abstract: | WIPI proteins, phosphatidylinositol 3-phosphate (PtdIns3P) binding proteins with β-propeller folds, are recruited to the omegasome following PtdIns3P production. The functions of the WIPI proteins in autophagosome formation are poorly understood. In a recent study, we reported that WIPI2B directly binds ATG16L1 and functions by recruiting the ATG12–ATG5-ATG16L1 complex to forming autophagosomes during starvation- or pathogen-induced autophagy. Our model of WIPI2 function provides an explanation for the PtdIns3P-dependent recruitment of the ATG12–ATG5-ATG16L1 complex during initiation of autophagy. |
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| Keywords: | ATG12– ATG5-ATG16L1, autophagosome, autophagy, omegasome, PtdIns3P, WIPI |
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