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Updated: Feb 16, 2026

A Fluorescence-based Assay of Phospholipid Scramblase Activity

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Published on: September 20, 2016

Phospholipid flipping involves a central cavity in P4 ATPases.

M S Jensen¹, S R Costa¹, A S Duelli²

¹Department of Plant and Environmental Sciences, University of Copenhagen, 1871, Frederiksberg, Denmark.

Scientific Reports

|December 17, 2017

Summary

P4 ATPase flippases move phospholipids across membranes. A new model suggests they use a central cavity, similar to cation pumps, to coordinate the phospholipid headgroup for transport.

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Published on: October 15, 2016

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

P4 ATPase flippases are crucial for establishing transmembrane lipid asymmetry.
The transport mechanism of P4 ATPases, unlike other P-type ATPases, remains unclear due to their large substrate.

Purpose of the Study:

To elucidate the mechanism of phospholipid translocation by P4 ATPases.
To generate a structural model for the broad-specificity flippase ALA10.

Main Methods:

Comparative modeling based on crystal structures of cation-transporting P-type ATPases.
In silico docking of phosphatidylcholine headgroups.
Mutagenesis studies to identify key residues.

Main Results:

A structural model of ALA10 revealed a cavity in the transmembrane domain.
This cavity can accommodate a phospholipid headgroup, with fatty acid tails oriented towards the bilayer.
Mutagenesis identified residues Y374 and F375 in TM4 as critical for headgroup coordination.

Conclusions:

P4 ATPases may translocate phospholipids via a mechanism analogous to cation pumps.
Coordination of the hydrophilic headgroup within a central membrane cavity is proposed.
This finding offers a general model for lipid translocation by P4 ATPases.