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Multivalent tumor suppressor adenomatous polyposis coli promotes Axin biomolecular condensate formation and efficient

Tie-Mei Li1,2,3, Jing Ren4, Dylan Husmann5

  • 1Department of Medicine, Stanford University School of Medicine, Stanford, CA, 94305, USA. tiemei.li2@gmail.com.

Scientific Reports
|October 16, 2020
PubMed

Insights

The adenomatous polyposis coli (APC) protein

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Biochemistry

Background:

  • The tumor suppressor adenomatous polyposis coli (APC) is frequently mutated in colorectal cancers.
  • APC is a key component of a protein complex that degrades beta-catenin, a protein implicated in oncogenesis.
  • The precise mechanism by which APC facilitates beta-catenin degradation remains unclear.

Purpose of the Study:

  • To investigate the molecular mechanism of APC-mediated beta-catenin degradation.
  • To explore the role of the intrinsically disordered region (IDR) of APC in this process.

Main Methods:

  • In vitro liquid-liquid phase separation (LLPS) assays using the APC IDR.
  • Cell-based assays in colorectal cancer cells to assess Axin puncta formation and beta-catenin levels upon expression of the APC IDR.

Main Results:

  • The APC IDR undergoes liquid-liquid phase separation (LLPS) in vitro.
  • Expression of the APC IDR in colorectal cells promotes the formation of Axin puncta.
  • APC IDR expression leads to enhanced degradation of beta-catenin.

Conclusions:

  • Multivalent interactions within the APC IDR drive the formation of biomolecular condensates.
  • These condensates concentrate components of the beta-catenin destruction complex, enhancing beta-catenin degradation.
  • This mechanism provides new insights into APC's tumor suppressor function in colorectal cancer.

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