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Updated: Sep 10, 2025

Oligopeptide Competition Assay for Phosphorylation Site Determination
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Oligopeptide Competition Assay for Phosphorylation Site Determination

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Phosphorylation-Mediated Regulation of FBXO31 Stability Under Cellular Homeostasis

Leijie Chen1,2,3, Jinyou Mo4, Jia Liu4

  • 1Department of Gastroenterology, The Second Xiangya Hospital of Central South University, Changsha, Hunan, 410011, China.

Advanced Biology
|August 23, 2025
PubMed

Insights

Phosphorylation regulates the stability of F-box-only protein 31 (FBXO31), a key regulator of genomic stability. Specific phosphorylation sites, Thr-37 and Ser-523, stabilize FBXO31, impacting its degradation and cellular functions.

Area of Science:

  • Molecular and Cellular Biology
  • Biochemistry
  • Genomics

Background:

  • F-box-only protein 31 (FBXO31) is an adaptor protein in SCF E3 ubiquitin ligase complexes.
  • FBXO31 plays critical roles in maintaining genomic stability and regulating cell signaling pathways.
  • Post-translational modifications, such as phosphorylation, are known to influence protein stability and function.

Purpose of the Study:

  • To identify and characterize the phosphorylation sites on FBXO31.
  • To investigate the impact of FBXO31 phosphorylation on its protein stability and degradation.
  • To elucidate the regulatory mechanisms governing FBXO31 stability and function.

Main Methods:

  • Biochemical and biological techniques were employed for site identification.
  • Liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to identify phosphorylated residues.
  • Western blotting, fluorescence-activated cell sorting (FACS), and cycloheximide experiments were utilized to assess protein stability.

Main Results:

  • Five FBXO31 phosphorylation sites were identified: Thr-28, Thr-37, Ser-33, Ser-400, and Ser-523.
  • Phosphorylation at Thr-37 and Ser-523 was found to stabilize FBXO31 protein.
  • Cycloheximide experiments confirmed that phosphorylation regulates FBXO31 turnover and degradation pathways.

Conclusions:

  • Phosphorylation is a critical regulatory mechanism for FBXO31 protein stability.
  • Specific phosphorylation sites, Thr-37 and Ser-523, are key determinants of FBXO31 stability.
  • Understanding FBXO31 phosphorylation provides insights into its physiological roles and potential therapeutic targets.
Keywords:
FBXO31protein phosphorylationstability

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