Structure and mechanism of ATP-dependent phospholipid transporters

ATP-binding cassette (ABC) transporters and P4-ATPases are two large and seemingly unrelated families of primary active pumps involved in moving phospholipids from one leaflet of a biological membrane to the other. This review aims to identify common mechanistic features in the way phospholipid flip...

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Published inBiochimica et biophysica acta Vol. 1850; no. 3; pp. 461 - 475
Main Authors López-Marqués, Rosa L., Poulsen, Lisbeth Rosager, Bailly, Aurélien, Geisler, Markus, Pomorski, Thomas Günther, Palmgren, Michael G.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.03.2015
Subjects
ABC transporter
ABC transporters
adenosine triphosphate
Adenosine Triphosphate - metabolism
adenosinetriphosphatase
Animals
Biological Transport
biophysics
Cell Membrane - metabolism
crystal structure
Flippase
Humans
hydrophobicity
Lipid flipping
Membrane Transport Proteins - chemistry
Membrane Transport Proteins - metabolism
Models, Molecular
P-type ATPase
P4-ATPase
Phospholipid Transfer Proteins - chemistry
Phospholipid Transfer Proteins - metabolism
phospholipids
Phospholipids - metabolism
Protein Conformation
pumps
Transport
Lipid flipping
Transport
P-type ATPase
ABC transporter
Flippase
P4-ATPase
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Abstract ATP-binding cassette (ABC) transporters and P4-ATPases are two large and seemingly unrelated families of primary active pumps involved in moving phospholipids from one leaflet of a biological membrane to the other. This review aims to identify common mechanistic features in the way phospholipid flipping is carried out by two evolutionarily unrelated families of transporters. Both protein families hydrolyze ATP, although they employ different mechanisms to use it, and have a comparable size with twelve transmembrane segments in the functional unit. Further, despite differences in overall architecture, both appear to operate by an alternating access mechanism and during transport they might allow access of phospholipids to the internal part of the transmembrane domain. The latter feature is obvious for ABC transporters, but phospholipids and other hydrophobic molecules have also been found embedded in P-type ATPase crystal structures. Taken together, in two diverse groups of pumps, nature appears to have evolved quite similar ways of flipping phospholipids. Our understanding of the structural basis for phospholipid flipping is still limited but it seems plausible that a general mechanism for phospholipid flipping exists in nature. This article is part of a Special Issue entitled Structural biochemistry and biophysics of membrane proteins. •Both ATP‐binding cassette (ABC) transporters and P4‐ATPases hydrolyze ATP but by different mechanisms.•Both families appear to operate by an alternating access mechanism for transmembrane flipping of phospholipids.•In two diverse groups of pumps, nature appears to have evolved in quite similar ways of flipping phospholipids.•It seems plausible that a general mechanism for phospholipid flipping exists in nature.
AbstractList ATP-binding cassette (ABC) transporters and P4-ATPases are two large and seemingly unrelated families of primary active pumps involved in moving phospholipids from one leaflet of a biological membrane to the other. This review aims to identify common mechanistic features in the way phospholipid flipping is carried out by two evolutionarily unrelated families of transporters. Both protein families hydrolyze ATP, although they employ different mechanisms to use it, and have a comparable size with twelve transmembrane segments in the functional unit. Further, despite differences in overall architecture, both appear to operate by an alternating access mechanism and during transport they might allow access of phospholipids to the internal part of the transmembrane domain. The latter feature is obvious for ABC transporters, but phospholipids and other hydrophobic molecules have also been found embedded in P-type ATPase crystal structures. Taken together, in two diverse groups of pumps, nature appears to have evolved quite similar ways of flipping phospholipids. Our understanding of the structural basis for phospholipid flipping is still limited but it seems plausible that a general mechanism for phospholipid flipping exists in nature. This article is part of a Special Issue entitled Structural biochemistry and biophysics of membrane proteins.
ATP-binding cassette (ABC) transporters and P4-ATPases are two large and seemingly unrelated families of primary active pumps involved in moving phospholipids from one leaflet of a biological membrane to the other.This review aims to identify common mechanistic features in the way phospholipid flipping is carried out by two evolutionarily unrelated families of transporters.Both protein families hydrolyze ATP, although they employ different mechanisms to use it, and have a comparable size with twelve transmembrane segments in the functional unit. Further, despite differences in overall architecture, both appear to operate by an alternating access mechanism and during transport they might allow access of phospholipids to the internal part of the transmembrane domain. The latter feature is obvious for ABC transporters, but phospholipids and other hydrophobic molecules have also been found embedded in P-type ATPase crystal structures. Taken together, in two diverse groups of pumps, nature appears to have evolved quite similar ways of flipping phospholipids.Our understanding of the structural basis for phospholipid flipping is still limited but it seems plausible that a general mechanism for phospholipid flipping exists in nature. This article is part of a Special Issue entitled Structural biochemistry and biophysics of membrane proteins.
ATP-binding cassette (ABC) transporters and P4-ATPases are two large and seemingly unrelated families of primary active pumps involved in moving phospholipids from one leaflet of a biological membrane to the other.BACKGROUNDATP-binding cassette (ABC) transporters and P4-ATPases are two large and seemingly unrelated families of primary active pumps involved in moving phospholipids from one leaflet of a biological membrane to the other.This review aims to identify common mechanistic features in the way phospholipid flipping is carried out by two evolutionarily unrelated families of transporters.SCOPE OF REVIEWThis review aims to identify common mechanistic features in the way phospholipid flipping is carried out by two evolutionarily unrelated families of transporters.Both protein families hydrolyze ATP, although they employ different mechanisms to use it, and have a comparable size with twelve transmembrane segments in the functional unit. Further, despite differences in overall architecture, both appear to operate by an alternating access mechanism and during transport they might allow access of phospholipids to the internal part of the transmembrane domain. The latter feature is obvious for ABC transporters, but phospholipids and other hydrophobic molecules have also been found embedded in P-type ATPase crystal structures. Taken together, in two diverse groups of pumps, nature appears to have evolved quite similar ways of flipping phospholipids.MAJOR CONCLUSIONSBoth protein families hydrolyze ATP, although they employ different mechanisms to use it, and have a comparable size with twelve transmembrane segments in the functional unit. Further, despite differences in overall architecture, both appear to operate by an alternating access mechanism and during transport they might allow access of phospholipids to the internal part of the transmembrane domain. The latter feature is obvious for ABC transporters, but phospholipids and other hydrophobic molecules have also been found embedded in P-type ATPase crystal structures. Taken together, in two diverse groups of pumps, nature appears to have evolved quite similar ways of flipping phospholipids.Our understanding of the structural basis for phospholipid flipping is still limited but it seems plausible that a general mechanism for phospholipid flipping exists in nature. This article is part of a Special Issue entitled Structural biochemistry and biophysics of membrane proteins.GENERAL SIGNIFICANCEOur understanding of the structural basis for phospholipid flipping is still limited but it seems plausible that a general mechanism for phospholipid flipping exists in nature. This article is part of a Special Issue entitled Structural biochemistry and biophysics of membrane proteins.
ATP-binding cassette (ABC) transporters and P4-ATPases are two large and seemingly unrelated families of primary active pumps involved in moving phospholipids from one leaflet of a biological membrane to the other. This review aims to identify common mechanistic features in the way phospholipid flipping is carried out by two evolutionarily unrelated families of transporters. Both protein families hydrolyze ATP, although they employ different mechanisms to use it, and have a comparable size with twelve transmembrane segments in the functional unit. Further, despite differences in overall architecture, both appear to operate by an alternating access mechanism and during transport they might allow access of phospholipids to the internal part of the transmembrane domain. The latter feature is obvious for ABC transporters, but phospholipids and other hydrophobic molecules have also been found embedded in P-type ATPase crystal structures. Taken together, in two diverse groups of pumps, nature appears to have evolved quite similar ways of flipping phospholipids. Our understanding of the structural basis for phospholipid flipping is still limited but it seems plausible that a general mechanism for phospholipid flipping exists in nature. This article is part of a Special Issue entitled Structural biochemistry and biophysics of membrane proteins. •Both ATP‐binding cassette (ABC) transporters and P4‐ATPases hydrolyze ATP but by different mechanisms.•Both families appear to operate by an alternating access mechanism for transmembrane flipping of phospholipids.•In two diverse groups of pumps, nature appears to have evolved in quite similar ways of flipping phospholipids.•It seems plausible that a general mechanism for phospholipid flipping exists in nature.
Author Poulsen, Lisbeth Rosager
Geisler, Markus
Palmgren, Michael G.
Bailly, Aurélien
Pomorski, Thomas Günther
López-Marqués, Rosa L.
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  email: rlo@plen.ku.dk
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  fullname: Poulsen, Lisbeth Rosager
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  givenname: Thomas Günther
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  fullname: Pomorski, Thomas Günther
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  surname: Palmgren
  fullname: Palmgren, Michael G.
  email: palmgren@plen.ku.dk
  organization: Centre for Membrane Pumps in Cells and Disease – PUMPkin, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark
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ID FETCH-LOGICAL-c531t-49c9cb2aff4619b3b378435068aa1fa33e939970033262c3038dd6b966d830c93
IEDL.DBID .~1
ISSN 0304-4165
0006-3002
IngestDate Fri Jul 11 06:50:16 EDT 2025
Fri Jul 11 02:25:56 EDT 2025
Thu Apr 03 07:08:43 EDT 2025
Tue Jul 01 00:22:03 EDT 2025
Thu Apr 24 23:11:28 EDT 2025
Fri Feb 23 02:32:42 EST 2024
IsPeerReviewed true
IsScholarly true
Issue 3
Keywords Lipid flipping
Transport
P-type ATPase
ABC transporter
Flippase
P4-ATPase
Language English
License Copyright © 2014 Elsevier B.V. All rights reserved.
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MergedId FETCHMERGED-LOGICAL-c531t-49c9cb2aff4619b3b378435068aa1fa33e939970033262c3038dd6b966d830c93
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PublicationTitle Biochimica et biophysica acta
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Snippet ATP-binding cassette (ABC) transporters and P4-ATPases are two large and seemingly unrelated families of primary active pumps involved in moving phospholipids...
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SubjectTerms ABC transporter
ABC transporters
adenosine triphosphate
Adenosine Triphosphate - metabolism
adenosinetriphosphatase
Animals
Biological Transport
biophysics
Cell Membrane - metabolism
crystal structure
Flippase
Humans
hydrophobicity
Lipid flipping
Membrane Transport Proteins - chemistry
Membrane Transport Proteins - metabolism
Models, Molecular
P-type ATPase
P4-ATPase
Phospholipid Transfer Proteins - chemistry
Phospholipid Transfer Proteins - metabolism
phospholipids
Phospholipids - metabolism
Protein Conformation
pumps
Transport
Title Structure and mechanism of ATP-dependent phospholipid transporters
URI https://dx.doi.org/10.1016/j.bbagen.2014.04.008
https://www.ncbi.nlm.nih.gov/pubmed/24746984
https://www.proquest.com/docview/1702653322
https://www.proquest.com/docview/2000222403
Volume 1850
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