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Updated: Jul 15, 2025

In Vitro Polymerization of F-actin on Early Endosomes
Published on: August 28, 2017
Vps60 initiates alternative ESCRT-III filaments
Anna-Katharina Pfitzner1, Henry Zivkovic1, César Bernat-Silvestre1
1Department of Biochemistry, University of Geneva, Geneva, Switzerland.
The study reveals that Vps60 and Snf7 form distinct Endosomal Sorting Complex Required for Transport-III (ESCRT-III) polymers. This subunit diversification likely enabled new cellular functions during evolution.
Area of Science:
- Cell Biology
- Molecular Biology
- Evolutionary Biology
Background:
- The Endosomal Sorting Complex Required for Transport-III (ESCRT-III) machinery is crucial for various cellular processes, including cell division and endosome maturation.
- Evolutionary diversification of ESCRT-III subunits may have led to novel cellular functions.
Purpose of the Study:
- To characterize a novel ESCRT-III copolymer initiated by Vps60.
- To investigate the functional distinctness of Vps60- and Snf7-based ESCRT-III polymers.
Main Methods:
- Investigated Vps60 polymerization and recruitment of downstream ESCRT-III subunits (Vps2, Vps24, Did2, Ist1).
- Utilized fibroblast cell models to compare the localization and recruitment dynamics of Vps60/CHMP5 and Snf7/CHMP4 during cellular functions.
- Examined recruitment during endosomal functions, cytokinesis, and nuclear envelope reformation.
Main Results:
- Vps60 forms membrane-bound polymers that recruit specific downstream subunits, similar to Snf7.
- Snf7- and Vps60-based filaments coexist on membranes but remain spatially and biochemically segregated.
- Vps60/CHMP5 and Snf7/CHMP4 exhibit distinct localization and recruitment dynamics during endosomal functions and cytokinesis, with Vps60/CHMP5 not recruited during nuclear envelope reformation.
Conclusions:
- Vps60 and Snf7 initiate functionally distinct ESCRT-III polymers.
- The diversification of ESCRT-III subunits is linked to the acquisition of new cellular functions.
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