Related Experiment Video

Updated: Feb 28, 2026

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein
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Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

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The G protein-coupled receptor GPR31 promotes membrane association of KRAS

Nicole Fehrenbacher1, Israel Tojal da Silva2, Craig Ramirez3

  • 1Perlmutter Cancer Center, New York University School of Medicine, New York, NY nfehren01@gmail.com.

The Journal of Cell Biology
|June 17, 2017
PubMed

Insights

G protein-coupled receptor 31 (GPR31) acts as a chaperone, escorting the KRAS4B protein to the plasma membrane. This interaction is crucial for KRAS4B

Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Biology

Background:

  • KRAS4B protein is a key driver of tumor growth, requiring plasma membrane association.
  • The precise mechanisms governing KRAS4B trafficking to the plasma membrane remain unclear.

Purpose of the Study:

  • To identify genes essential for KRAS4B plasma membrane association.
  • To elucidate the role of GPR31 in KRAS4B trafficking and function.

Main Methods:

  • Genome-wide genetic screen to identify novel interacting genes.
  • Cellular localization studies using microscopy.
  • Gene silencing experiments to assess functional impact.

Main Results:

  • G protein-coupled receptor 31 (GPR31) was identified as a novel binding partner for KRAS4B.
  • GPR31 mediates KRAS4B plasma membrane association in a farnesylation-dependent manner.
  • GPR31 silencing impairs KRAS4B trafficking, slows tumor cell growth, and inhibits macropinocytosis.

Conclusions:

  • GPR31 functions as a secretory pathway chaperone for KRAS4B.
  • Targeting GPR31 may offer a therapeutic strategy for KRAS-driven cancers.

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