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Article

The beta domain is required for Vps4p oligomerization into a functionally active ATPase.

The FEBS journal - 1 Jun 2006

Vajjhala Parimala R, Wong Julin S, To Hui-Yi, Munn Alan L

Abstract excerpt

Endocytic and biosynthetic trafficking pathways to the lysosome/vacuole converge at the prevacuolar endosomal compartment. During transport through this compartment, integral membrane proteins that are destined for delivery to the lysosome/vacuole lumen undergo multivesicular body (MVB) sorting into internal vesicles formed by invagination of the endosomal limiting membrane. Vps4 is an AAA family ATPase which...

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Identifiers

PMID: 16704411
DOI: 10.1111/j.1742-4658.2006.05238.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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The beta domain is required for Vps4p oligomerization into a functionally active ATPase.PMID 16704411Read ↗

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Structural and mechanistic studies of VPS4 proteins.Semantic proximity Read ↗

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Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p.Semantic proximity Read ↗

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Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p.Semantic proximity Read ↗

Mammalian class E Vps proteins, SBP1 and mVps2/CHMP2A, interact with and regulate the function of an AAA-ATPase SKD1/Vps4B.Semantic proximity Read ↗

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Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae.Semantic proximity Read ↗

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