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Related Experiment Video

Updated: Jul 6, 2026

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 8, 2013

ESCRT-III recognition by VPS4 ATPases.

Melissa D Stuchell-Brereton¹, Jack J Skalicky, Collin Kieffer

¹Department of Biochemistry, Room 4100, 15 N. Medical Drive East, University of Utah, Salt Lake City, Utah 84112-5650, USA.

|October 12, 2007

Summary

Researchers discovered how VPS4 ATPases recognize ESCRT-III proteins (CHMP) to drive membrane fission for HIV budding, endosomal sorting, and cell division. This mechanism is crucial for releasing viruses, vesicles, and daughter cells.

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Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

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Published on: December 21, 2019

Area of Science:

Cell Biology
Molecular Biology
Virology

Background:

The endosomal sorting complex required for transport (ESCRT) pathway is vital for membrane fission in processes like HIV budding and cytokinesis.
VPS4 ATPases are key to this pathway, disassembling ESCRT-III complexes at membranes.

Purpose of the Study:

To elucidate the molecular mechanism by which VPS4 ATPases recognize and interact with ESCRT-III proteins.
To understand how this interaction facilitates membrane fission events.

Main Methods:

Structural analysis of VPS4A MIT-CHMP1A and VPS4B MIT-CHMP2B complexes.
Site-directed mutagenesis to investigate binding interactions.
Functional assays assessing VPS4 recruitment, endosomal sorting, and HIV budding.

Main Results:

The microtubule interacting and transport (MIT) domains of VPS4A and VPS4B bind conserved motifs in CHMP1-3 proteins.
Structural studies revealed a unique binding mode of the CHMP motif within the VPS4 MIT domain.
Mutations disrupting this interaction impaired VPS4 function in multiple cellular processes.

Conclusions:

VPS4 ATPases recognize CHMP substrates through specific interactions within the MIT domain.
This recognition mechanism is essential for mediating membrane fission in viral release, endosomal trafficking, and cell division.