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Vacuolar-type H+-translocating ATPase (V-ATPase) dysfunction activates a unique autophagy pathway. Tryptophan metabolism inhibits this V-ATPase-dependent autophagy through ribosome biogenesis and NAD+ synthesis.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The vacuolar-type H+-translocating ATPase (V-ATPase) is generally considered essential for autophagy.
  • Mutations in V-ATPase linked to follicular lymphoma cause lysosomal deacidification and increased autophagy, despite unclear mechanisms.

Purpose of the Study:

  • To elucidate the mechanisms by which V-ATPase dysfunction activates autophagy.
  • To investigate the regulation of this novel V-ATPase-dependent autophagy pathway.

Main Methods:

  • Transcriptomic and proteomic profiling in yeast.
  • Genome-wide suppressor screening.
  • Analysis of tryptophan metabolism and its effectors.

Main Results:

  • V-ATPase dysfunction induces a selective autophagy flux, termed V-ATPase-dependent autophagy, distinct from starvation-induced autophagy.
  • Tryptophan metabolism negatively regulates V-ATPase-dependent autophagy via two pathways.
  • Tryptophan metabolism represses Gcn4/ATF4 translation by activating ribosome biogenesis and inhibits autophagy by fueling NAD+ biosynthesis.

Conclusions:

  • V-ATPase dysfunction activates a unique autophagy pathway regulated by tryptophan metabolism.
  • This pathway provides a mechanistic explanation for elevated autophagy in follicular lymphoma patients with V-ATPase mutations.