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Vps68 cooperates with ESCRT-III in intraluminal vesicle formation

Sören Alsleben1, Ralf Kölling1

  • 1Institut für Lebensmittelwissenschaft und Biotechnologie, Fg. Hefegenetik und Gärungstechnologie, Universität Hohenheim, 70599 Stuttgart, Germany.

Journal of Cell Science
|April 21, 2022
PubMed

Insights

Vps68 protein cooperates with the ESCRT-III complex to form intraluminal vesicles (ILVs) within endosomes. Deleting VPS68 impairs ILV formation, suggesting Vps68

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Interactions

Background:

  • The endosomal sorting complex required for transport (ESCRT)-III machinery is crucial for forming intraluminal vesicles (ILVs) within multivesicular endosomes.
  • Mos10 (Vps60) is an ESCRT-III-associated protein involved in ILV formation.

Purpose of the Study:

  • To investigate the function of the newly identified Vps68 protein in ILV formation.
  • To elucidate the interaction between Vps68 and the ESCRT-III complex.

Main Methods:

  • Stable isotope labeling of amino acids in cell culture (SILAC) coupled with mass spectrometry to identify Vps68 interaction partners.
  • Analysis of VPS68 deletion strains to assess ILV formation and ESCRT-III composition.

Main Results:

  • Vps68 was identified as a novel interaction partner of the ESCRT-III pathway.
  • VPS68 deletion resulted in sorting defects similar to SNF7 deletion under high cargo load.
  • ESCRT-III composition was altered in VPS68 deletion strains, with increased core components and decreased associated proteins.
  • Vps68 exhibits an unusual membrane topology with amphipathic helices on the luminal side of the endosomal membrane.

Conclusions:

  • Vps68 cooperates with ESCRT-III in ILV formation, potentially by weakening membrane leaflets during abscission.
  • The findings suggest a role for Vps68 in regulating ESCRT-III function and membrane remodeling during ILV biogenesis.
Keywords:
EndocytosisIntraluminal vesiclesMultivesicular body

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