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PTPRS Regulates Colorectal Cancer RAS Pathway Activity by Inactivating Erk and Preventing Its Nuclear Translocation

Thomas B Davis1, Mingli Yang1, Michael J Schell2

  • 1Gibbs Cancer Center & Research Institute, 380 Serpentine Drive, Spartanburg, SC, 29303, USA.

Scientific Reports
|June 20, 2018
PubMed

Insights

Colorectal cancer (CRC) progression involves RAS pathway activation. Protein tyrosine phosphatase PTPRS regulates this pathway by modulating ERK signaling, with mutations potentially increasing cancer signaling.

Area of Science:

  • Oncology
  • Molecular Biology
  • Cancer Research

Background:

  • Colorectal cancer (CRC) growth is often driven by RAS pathway activation.
  • This activation typically occurs via growth factor receptors or KRAS/BRAF mutations.

Purpose of the Study:

  • To investigate an additional mechanism of RAS pathway modulation in CRC.
  • To explore the role of PTPRS in regulating RAS pathway signaling.

Main Methods:

  • Investigated the interaction between PTPRS and the RAS pathway.
  • Analyzed PTPRS's effect on ERK phosphorylation and nuclear translocation.
  • Examined the impact of native PTPRS mutations found in CRC.

Main Results:

  • PTPRS, a protein tyrosine phosphatase, regulates RAS pathway activation through ERK.
  • PTPRS modulates ERK phosphorylation and its subsequent translocation to the nucleus.
  • Native PTPRS mutations (~10% of CRC) may decrease phosphatase activity, leading to increased ERK activation.

Conclusions:

  • PTPRS represents a novel regulatory mechanism for the RAS pathway in colorectal cancer.
  • PTPRS mutations may contribute to CRC progression by enhancing ERK-mediated transcriptional signaling.

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