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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
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DNA Framework-Based Lysosome-Targeting Chimeras: Intracellular ATP-Facilitated Extracellular Protein Degradation.

Yujun Ning1, Bin Li1, Weishuai Chen1

  • 1Department of Chemistry, Shanghai Stomatological Hospital, State Key Laboratory of Molecular Engineering of Polymers and Institute of Biomedical Sciences, Fudan University, Shanghai 200433, People's Republic of China.

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Summary

This study introduces tetrahedral DNA framework-based lysosome-targeting chimeras (TDF-LYTACs) for targeted protein degradation. These TDF-LYTACs link extracellular protein degradation to intracellular adenosine triphosphate (ATP) levels.

Keywords:
ATP sensing and imagingextracellular proteinstargeted chimerastargeted degradationtetrahedral DNA framework

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Nanotechnology

Background:

  • Targeted protein degradation (TPD) is a therapeutic strategy for eliminating disease-causing proteins, including those previously considered undruggable.
  • Adenosine triphosphate (ATP) is crucial for cellular functions and is stored in lysosomes, which are key organelles for degradation.
  • Understanding the interplay between extracellular protein degradation and intracellular ATP dynamics is essential for developing novel therapeutic approaches.

Purpose of the Study:

  • To develop and characterize the first dual-function tetrahedral DNA framework-based lysosome-targeting chimeras (TDF-LYTACs).
  • To investigate the correlation between lysosomal degradation of extracellular proteins and intracellular ATP level fluctuations.
  • To visualize and quantify the degradation of platelet-derived growth factor (PDGF) and simultaneous changes in ATP levels.

Main Methods:

  • Construction of multifunctional TDF-LYTACs using a PDGF aptamer, an APE1-triggered ATP probe, and an IGFII receptor (IGFIIR) ligand.
  • Utilizing TDF-LYTACs to target PDGF for lysosomal degradation.
  • Synchronous visualization and quantification of PDGF degradation and intracellular ATP levels.

Main Results:

  • TDF-LYTACs efficiently facilitated the lysosomal degradation of PDGF.
  • A significant positive correlation was observed between PDGF degradation efficiency and intracellular ATP levels.
  • The study demonstrated the capability of TDF-LYTACs to simultaneously degrade proteins and monitor ATP fluctuations.

Conclusions:

  • TDF-LYTACs represent a novel platform for dual-function extracellular protein degradation and ATP level monitoring.
  • The findings highlight a direct relationship between lysosomal degradation efficiency and intracellular ATP availability.
  • This versatile TDF-LYTAC system offers a promising perspective for targeting multifunctional extracellular proteins and understanding cellular energy dynamics.