Flippases: still more questions than answers |
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Authors: | L R Poulsen R L López-Marqués M G Palmgren |
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Institution: | (1) Centre for Membrane Pumps in Cells and Disease – PUMPKIN, Danish National Research Foundation, Department of Plant Biology and Biotechnology, University of Copenhagen, Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark |
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Abstract: | Our understanding of flippase-mediated lipid translocation and membrane vesiculation, and the involvement of P-type ATPases
in these processes is just beginning to emerge. The results obtained so far demonstrate significant complexity within this
field and point to major tasks for future research. Most importantly, biochemical characterization of P4-ATPases is required in order to clarify whether these transporters indeed are capable of catalyzing transmembrane phospholipid
flipping. The β-subunit of P4-ATPases shows unexpected similarities between the β- and γ-subunits of the Na+/K+-ATPase. It is likely that these proteins provide a similar solution to similar problems, and might have adopted similar structures
to accomplish these tasks. No P4-ATPases have been identified in the endoplasmic reticulum and it remains an intriguing possibility that, in this compartment,
P5A-ATPases are functional homologues of P4-ATPases.
Received 19 June 2008; received after revision 31 July 2008; accepted 15 August 2008 |
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Keywords: | " target="_blank"> Flippases vesicle formation phospholipid flipping P4-ATPases P5A-ATPases |
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