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TRIM25 dictates selective miRNA loading into extracellular vesicles during inflammation

Kayla E King1,2, Priyanka Ghosh1,2, Ann L Wozniak3,4

  • 1Department of Internal Medicine, University of Kansas Medical Center, Mailstop 1018, Kansas City, KS, 66160, USA.

Scientific Reports
|December 22, 2023
PubMed

Insights

Inflammation promotes the loading of RNA-binding protein FMR1 and microRNA miR-155 into extracellular vesicles (EVs). This process is controlled by the E3 ligase TRIM25, which ubiquitinates FMR1, impacting EV biogenesis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Extracellular vesicles (EVs) mediate cell-to-cell communication via specific biomolecules.
  • Understanding selective EV cargo loading is crucial for deciphering physiological and pathological roles.

Purpose of the Study:

  • To identify novel mechanisms regulating inflammation-mediated cargo loading into EVs.
  • To investigate the role of E3 ligase TRIM25 in the EV loading of FMR1 and miR-155.

Main Methods:

  • Investigated the interaction between TRIM25, FMR1, and RILP.
  • Utilized knockdown of TRIM25 to assess its effect on FMR1 and miR-155 EV loading.
  • Analyzed K63-ubiquitination of FMR1.

Main Results:

  • TRIM25 targets FMR1 for K63-ubiquitination, promoting its interaction with the EV loading machinery via RILP.
  • TRIM25 knockdown disrupts FMR1-RILP interaction and prevents FMR1 and miR-155 loading into EVs.
  • Demonstrated TRIM25's critical role in inflammation-mediated EV cargo selection.

Conclusions:

  • TRIM25-mediated ubiquitination of FMR1 is essential for inflammation-induced EV loading of FMR1 and miR-155.
  • Findings provide insights into EV biogenesis regulation and potential therapeutic targets.

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