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Setting a Successful Sorting for Extracellular Vesicle Isolation
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UBL3 modification influences protein sorting to small extracellular vesicles.

Hiroshi Ageta1,2, Natsumi Ageta-Ishihara3, Keisuke Hitachi1

  • 1Division for Therapies Against Intractable Diseases, Institute for Comprehensive Medical Science, Fujita Health University, 1-98 Dengakugakubo, Kutsukake-cho, Toyoake, Aichi, 470-1192, Japan.

Nature Communications
|September 28, 2018
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Ubiquitin-like 3 (UBL3) acts as a posttranslational modification factor, regulating protein sorting into small extracellular vesicles (sEVs). UBL3 modification is crucial for targeting proteins like Ras to sEVs, impacting cell communication.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Small extracellular vesicles (sEVs) mediate intercellular communication via cargo transfer.
  • Mechanisms governing protein sorting into sEVs remain incompletely understood.
  • Posttranslational modifications (PTMs) are increasingly recognized as regulators of protein localization.

Purpose of the Study:

  • To investigate the role of ubiquitin-like 3 (UBL3) in protein sorting to sEVs.
  • To identify UBL3-interacting proteins and characterize UBL3-mediated modifications.
  • To elucidate the impact of UBL3 on the secretion of specific proteins, such as Ras, into sEVs.

Main Methods:

  • Generation and analysis of Ubl3-knockout mice.
  • Proteomics analysis to identify UBL3-interacting proteins.
  • In vitro modification assays to assess UBL3's effect on Ras and its mutants.

Main Results:

  • UBL3 functions as a PTM factor regulating protein sorting into sEVs.
  • UBL3 modification is essential for UBL3's own sorting into multivesicular bodies (MVBs) and sEVs.
  • Ubl3 knockout significantly reduced total protein content in sEVs.
  • Proteomics identified 1241 UBL3-interacting proteins, including Ras.
  • UBL3 directly modifies Ras and the oncogenic RasG12V mutant, enhancing RasG12V sorting into sEVs.

Conclusions:

  • PTM by UBL3 is a key mechanism influencing protein sorting into sEVs.
  • UBL3 plays a critical role in regulating the composition of sEVs.
  • Targeting UBL3-mediated pathways may offer novel strategies for modulating sEV cargo and function.