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

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.

Pubmed ID: 19270696

Authors

  • Matsunaga K
  • Saitoh T
  • Tabata K
  • Omori H
  • Satoh T
  • Kurotori N
  • Maejima I
  • Shirahama-Noda K
  • Ichimura T
  • Isobe T
  • Akira S
  • Noda T
  • Yoshimori T

Journal

Nature cell biology

Publication Data

April 1, 2009

Associated Grants

None

Mesh Terms

  • Adaptor Proteins, Vesicular Transport
  • Animals
  • Apoptosis Regulatory Proteins
  • Autophagy
  • Cell Line, Tumor
  • Endocytosis
  • Green Fluorescent Proteins
  • Humans
  • Membrane Proteins
  • Mice
  • Microtubule-Associated Proteins
  • Multiprotein Complexes
  • Phagosomes
  • Protein Binding
  • Protein Processing, Post-Translational
  • RNA, Small Interfering
  • Recombinant Fusion Proteins