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Shaping membranes into autophagosomes

Nature Cell Biology volume 9, pages 1125–1127 (2007)Cite this article

The class III phosphatidylinositol 3-kinase (PI(3)KC3) is part of a key complex regulating autophagy. How this complex mechanistically contributes to autophagosome formation remains largely unknown. The BAR-domain-containing protein Bif-1/endophilin B1, commonly associated with the control of membrane curvature, has been identified as a new interacting partner for PI(3)KC3, suggesting the complex plays an active part in the regulation of membrane dynamics during autophagy.

Despite the identification in Saccharomyces cerevisiae of the 17 autophagy (Atg) genes that constitute the basic machinery for autophagosome biogenesis in all eukaryotes, the origin of the phagophore and its expansion mode are unknown. Two of the Atg gene products, Atg6 and Atg14, together with Vps15 and PI(3)K Vps34, form the yeast PI(3)K complex I (yPI(3)K-CI) (Fig. 1b)5. This complex is one of the first components to be recruited to the forming autophagosome and is essential for autophagy (Fig. 1b)5,6. Vps34, Vps15 and Atg6 are also found in a second complex, yPI(3)K-CII, which is exclusively devoted to endosomal trafficking and in which Atg14 is substituted by Vps38 (Fig. 1b)5.

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Figure 1: Autophagosome biogenesis and PI(3)K activities.
Figure 2: Schematic representation of Bif-1 indicating all the known Bif-1 interactors and the Bif-1 domain that they bind to.

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  1. Muriel Mari and Fulvio Reggiori are at the Department of Cell Biology and Institute of Biomembranes, University Medical Center Utrecht, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands. F.Reggiori@umcutrecht.nl

    Muriel Mari & Fulvio Reggiori

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  1. Muriel Mari
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  2. Fulvio Reggiori
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Mari, M., Reggiori, F. Shaping membranes into autophagosomes. Nat Cell Biol 9, 1125–1127 (2007). https://doi.org/10.1038/ncb1007-1125

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