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Related Experiment Videos

Membrane transport: ubiquitylation in endosomal sorting.

S Dupré1, C Volland, R Haguenauer-Tsapis

  • 1Institut Jacques Monod, Universités Paris VI and Paris VII, 2 place Jussieu, 75251 PARIS Cedex 05, France.

Current Biology : CB
|November 24, 2001
PubMed
Summary

Ubiquitylation targets membrane proteins for sorting into vesicles in yeast late endosomes. A conserved protein complex, including yeast Vps23p or mammalian Tsg101, may function as the ubiquitin receptor.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Membrane protein sorting is crucial for cellular function.
  • Late endosomes generate multivesicular bodies via inward-budding vesicles.
  • Ubiquitylation plays a key role in protein trafficking and degradation.

Purpose of the Study:

  • To investigate the mechanism of membrane protein sorting in yeast.
  • To identify the ubiquitin receptor involved in vesicle formation at late endosomes.

Main Methods:

  • Yeast genetics and molecular biology techniques.
  • Protein complex analysis.
  • Ubiquitylation assays.

Main Results:

  • Membrane proteins require ubiquitylation for proper sorting into vesicles.

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  • A conserved protein complex, Vps23p/Tsg101, is implicated in this process.
  • This complex may function as a ubiquitin receptor for cargo selection.

    • Conclusions:

    • Ubiquitylation is essential for targeting membrane proteins to multivesicular bodies in yeast.
    • The Vps23p/Tsg101 complex is a likely candidate for the ubiquitin receptor mediating this sorting event.