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Glucose-mediated N-glycosylation of RPTPα affects its subcellular localization and Src activation

Jiayu Fang1, Yuqin Zhang1, Caihu Huang1

  • 1Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-SM), Shanghai, 200025, China.

Oncogene
|February 10, 2023
PubMed

Insights

Receptor-type protein tyrosine phosphatase α (RPTPα) undergoes N-glycosylation, altering its location and enhancing Src activation. This discovery links glucose levels to tumor development and offers potential new cancer therapies.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Receptor-type protein tyrosine phosphatase α (RPTPα) is crucial in cellular processes and cancer.
  • RPTPα regulates Src activation, a key oncogene, but its post-translational modifications remain unclear.

Purpose of the Study:

  • To investigate the post-translational modifications of RPTPα.
  • To understand how these modifications influence RPTPα's function in cancer development.

Main Methods:

  • Identification of N-glycosylation sites on the extracellular segment of RPTPα.
  • Analysis of RPTPα localization and interaction with Src under varying glucose concentrations.

Main Results:

  • RPTPα is N-glycosylated at specific sites (N21, N36, N68, N80, N86, N104, N124).
  • Glucose concentration-dependent N-glycosylation alters RPTPα localization from the Golgi to the plasma membrane.
  • This modification enhances RPTPα interaction with Src, increasing Src activation and promoting tumor development.

Conclusions:

  • N-glycosylation of RPTPα is a critical regulatory mechanism.
  • The link between glucose levels, RPTPα N-glycosylation, Src activation, and tumor promotion is established.
  • These findings offer novel therapeutic targets for antitumor strategies.

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