ArticleFEBS letters2026
Linked dimers of the AAA+ ATPase Msp1 reveal energetic demands and mechanistic plasticity for substrate extraction from lipid bilayers.
Article in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Lipid bilayer properties govern substrate engagement and extraction by the AAA+ ATPase Msp1.The Journal of biological chemistry · 2025Article
- The AAA+ protein Msp1 recognizes substrates by a hydrophobic mismatch.bioRxiv : the preprint server for biology · 2024Article
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6 authors.
Funding
Abstract
Msp1 is a membrane-anchored AAA+ (ATPases Associated with diverse cellular Activities) enzyme that extracts membrane proteins from lipid bilayers. To understand how the subunits in the homohexamer convert ATP hydrolysis into mechanical work, we developed covalently linked dimers combining wild-type and catalytically inactive (E193Q) subunits. These assembled into pseudohexameric trimers of dimers and retained ATPase activity, indicating that E193Q does not act as a dominant negative for ATP hydrolysis. Conversely, substrate extraction was impaired in some constructs, suggesting position-specific effects. Surprisingly, constructs with a twofold difference in ATPase rates showed minimal differences in substrate extraction across lipid environments, suggesting excess ATPase capacity. These findings clarify how Msp1 coordinates hydrolysis, its energetic requirements, and substrate access to the pore.
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