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FIP200 regulates targeting of Atg16L1 to the isolation membrane
Author(s) -
Nishimura Taki,
Kaizuka Takeshi,
Cadwell Ken,
Sahani Mayurbhai H,
Saitoh Tatsuya,
Akira Shizuo,
Virgin Herbert W,
Mizushima Noboru
Publication year - 2013
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2013.6
Subject(s) - atg16l1 , autophagy , autophagosome , ulk1 , microbiology and biotechnology , phosphatidylinositol , membrane , chemistry , biology , kinase , biochemistry , protein kinase a , apoptosis , ampk
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.