JOURNAL ARTICLE

Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages

Kohichi Matsunaga, Tatsuya Saitoh, Keisuke Tabata, Hiroko Omori, Takashi Satoh, Naoki Kurotori, Ikuko Maejima, Kanae Shirahama-Noda, Tohru Ichimura, Toshiaki Isobe, Shizuo Akira, Takeshi Noda, Tamotsu Yoshimori
Nature Cell Biology 2009, 11 (4): 385-96
19270696
Beclin 1, a protein essential for autophagy, binds to hVps34/Class III phosphatidylinositol-3-kinase and UVRAG. Here, we have identified two Beclin 1 associated proteins, Atg14L and Rubicon. Atg14L and UVRAG bind to Beclin 1 in a mutually exclusive manner, whereas Rubicon binds only to a subpopulation of UVRAG complexes; thus, three different Beclin 1 complexes exist. GFP-Atg14L localized to the isolation membrane and autophagosome, as well as to the ER and unknown puncta. Knockout of Atg14L in mouse ES cells caused a defect in autophagosome formation. GFP-Rubicon was localized at the endosome/lysosome. Knockdown of Rubicon caused enhancement of autophagy, especially at the maturation step, as well as enhancement of endocytic trafficking. These data suggest that the Beclin 1-hVps34 complex functions in two different steps of autophagy by altering the subunit composition.

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