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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Golgi apparatus (GA) is central to intracellular trafficking.
  • Targeting the GA selectively presents a significant challenge in cell biology.

Purpose of the Study:

  • To develop a novel method for selectively targeting the Golgi apparatus.
  • To investigate the mechanism of targeting and its downstream effects on cellular processes.

Main Methods:

  • Utilized unconventional peptide thioesters as novel GA-targeting agents.
  • Investigated cellular uptake mechanisms (caveolin-mediated endocytosis, macropinocytosis) based on concentration.
  • Analyzed thiopeptide hydrolysis by GA-associated thioesterases and subsequent dimerization and accumulation.
  • Examined the impact of GA and ER accumulation on protein trafficking and cell viability.
  • Tested targeting ability across various cell types (human, murine, *Drosophila*) and with modified peptide structures.

Main Results:

  • Peptide thioesters effectively target the Golgi apparatus in various cell types.
  • Hydrolysis by thioesterases leads to thiopeptide accumulation in the GA and ER.
  • Accumulation disrupts protein trafficking and induces cell death through multiple pathways.
  • Targeting the GA influences the distribution of proteins like NRAS.
  • Modifications like using l-diphenylalanine maintain GA-targeting ability.

Conclusions:

  • Developed a thioesterase-responsive molecular platform for GA targeting.
  • Demonstrated the ability to control cellular fates by manipulating GA and ER protein levels.
  • This approach offers a new strategy for intracellular trafficking modulation and therapeutic development.