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PIK3C3/VPS34 control by acetylation.

Hua Su1, Wei Liu1,2

  • 1a Department of Biochemistry and Molecular Biology , Zhejiang University School of Medicine , Hangzhou , Zhejiang , China.

Autophagy
|October 6, 2017
PubMed
Summary
This summary is machine-generated.

A novel acetylation-deacetylation switch regulates PIK3C3/VPS34 activity, crucial for autophagy and membrane transport. This mechanism, controlled by EP300, activates PIK3C3/VPS34 independently of common pathways like AMPK and MTORC1.

Keywords:
VPS34acetylationautophagyendocytic transportp300

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • PIK3C3/VPS34 enzyme activity is essential for macroautophagy and endosomal transport.
  • Activation was previously thought to solely depend on core complex assembly at membranes.

Purpose of the Study:

  • To elucidate a novel regulatory mechanism for PIK3C3/VPS34 activation.
  • To investigate the role of acetylation and deacetylation in controlling PIK3C3/VPS34 function.

Main Methods:

  • In vitro enzymatic assays.
  • Cellular studies using genetic and biochemical approaches.
  • Analysis of protein acetylation and deacetylation modifications.

Main Results:

  • EP300-mediated acetylation represses PIK3C3/VPS34 activity under nutrient-rich conditions.
  • Nutrient deprivation leads to deacetylation and PIK3C3/VPS34 activation.
  • Deacetylation at K771 is critical for substrate binding and full enzyme activation.
  • This pathway is utilized in starvation-induced and other forms of autophagy.

Conclusions:

  • EP300-dependent acetylation/deacetylation acts as a molecular switch for PIK3C3/VPS34.
  • This novel activation circuit bypasses canonical AMPK, MTORC1, and ULK1 pathways.
  • The findings reveal a new mechanism for regulating membrane dynamics in response to cellular cues.