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The Crossmodal Congruency Task as a Means to Obtain an Objective Behavioral Measure in the Rubber Hand Illusion Paradigm
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Binding Rubicon to cross the Rubicon

Kohichi Matsunaga1, Takeshi Noda, Tamotsu Yoshimori

  • 1Department of Cellular Regulation, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.

Autophagy
|June 25, 2009
PubMed

Insights

Beclin 1 interacts with Atg14L or UVRAG/Rubicon to regulate autophagy. These distinct protein complexes determine whether the Beclin 1-Vps34-Vps15 complex promotes or inhibits autophagy and endocytosis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Beclin 1 is a crucial protein for mammalian autophagy, but its exact molecular role remains unclear.
  • Understanding Beclin 1's interactions is key to elucidating its function in cellular processes.

Purpose of the Study:

  • To identify novel Beclin 1-interacting proteins.
  • To characterize the molecular mechanisms by which Beclin 1 regulates autophagy and endocytosis.

Main Methods:

  • Mass spectrometry was employed to identify proteins interacting with Beclin 1.
  • Immunofluorescence was used to determine the subcellular localization of protein complexes.

Main Results:

  • Two novel proteins, Atg14L and Rubicon, were found to associate with Beclin 1, alongside UVRAG.
  • Atg14L forms a complex that positively regulates early autophagy and localizes to the phagophore, autophagosome, and ER.
  • The Rubicon-UVRAG complex negatively regulates later autophagy and the endocytic pathway, localizing to late endosomes/lysosomes.

Conclusions:

  • The Beclin 1-Vps34-Vps15 core complex is a versatile regulator of both autophagy and the endocytic pathway.
  • The specific function of this complex is dictated by its interacting subunits, Atg14L or UVRAG/Rubicon.
  • This discovery provides critical insights into the context-dependent roles of Beclin 1 in cellular regulation.

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