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- Title
Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages.
- Authors
Matsunaga, Kohichi; Saitoh, Tatsuya; Tabata, Keisuke; Omori, Hiroko; Satoh, Takashi; Kurotori, Naoki; Maejima, Ikuko; Shirahama-Noda, Kanae; Ichimura, Tohru; Isobe, Toshiaki; Akira, Shizuo; Noda, Takeshi; Yoshimori, Tamotsu
- Abstract
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.
- Publication
Nature cell biology, 2009, Vol 11, Issue 4, p385
- ISSN
1476-4679
- Publication type
Journal Article
- DOI
10.1038/ncb1846