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Self-interaction is critical for Atg9 transport and function at the phagophore assembly site during autophagy.

Autophagy is the degradation of a cell's own components within lysosomes (or the analogous yeast vacuole), and its malfunction contributes to a variety of human diseases. Atg9 is the sole integral membrane protein required in formation of the initial sequestering compartment, the phagophore, and is proposed to play a key role in membrane transport; the phagophore presumably expands by vesicular addition to form a complete autophagosome. It is not clear through what mechanism Atg9 functions at the phagophore assembly site (PAS). Here we report that Atg9 molecules self-associate independently of other known autophagy proteins in both nutrient-rich and starvation conditions. Mutational analyses reveal that self-interaction is critical for anterograde transport of Atg9 to the PAS. The ability of Atg9 to self-interact is required for both selective and nonselective autophagy at the step of phagophore expansion at the PAS. Our results support a model in which Atg9 multimerization facilitates membrane flow to the PAS for phagophore formation.

Pubmed ID: 18829864


  • He C
  • Baba M
  • Cao Y
  • Klionsky DJ


Molecular biology of the cell

Publication Data

December 1, 2008

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM53396

Mesh Terms

  • Amino Acid Sequence
  • Aminopeptidases
  • Autophagy
  • DNA Mutational Analysis
  • Humans
  • Membrane Proteins
  • Molecular Sequence Data
  • Organisms, Genetically Modified
  • Phagosomes
  • Point Mutation
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins