FIP200 regulates targeting of Atg16L1 to the isolation membrane
Autophagosome formation is a dynamic process that is strictly controlled by autophagy‐related (Atg) proteins. However, how these Atg proteins are recruited to the autophagosome formation site or autophagic membranes remains poorly understood. Here, we found that FIP200, which is involved in proximal...
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Veröffentlicht in: | EMBO reports 2013-03, Vol.14 (3), p.284-291 |
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Sprache: | eng |
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Zusammenfassung: | Autophagosome formation is a dynamic process that is strictly controlled by autophagy‐related (Atg) proteins. However, how these Atg proteins are recruited to the autophagosome formation site or autophagic membranes remains poorly understood. Here, we found that FIP200, which is involved in proximal events, directly interacts with Atg16L1, one of the downstream Atg factors, in an Atg14‐ and phosphatidylinositol 3‐kinase‐independent manner. Atg16L1 deletion mutants, which lack the FIP200‐interacting domain, are defective in proper membrane targeting. Thus, FIP200 regulates not only early events but also late events of autophagosome formation through direct interaction with Atg16L1.
This report shows that FIP200 and Atg16L1, mediators of the early and late steps in the autophagy pathway respectively, physically interact, and that this interaction is important for targeting of Atg16L1 to the isolation membrane. |
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ISSN: | 1469-221X 1469-3178 |
DOI: | 10.1038/embor.2013.6 |