Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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


  • 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


Nature cell biology

Publication Data

April 1, 2009

Associated Grants


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