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Related Concept Videos

Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
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ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

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ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
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ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

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The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

10.5K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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ATP Synthase: Structure01:18

ATP Synthase: Structure

16.9K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

5.1K
V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
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Related Experiment Video

Updated: Mar 17, 2026

A Fluorescence-based Assay of Phospholipid Scramblase Activity
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A Fluorescence-based Assay of Phospholipid Scramblase Activity

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P4-ATPases as Phospholipid Flippases-Structure, Function, and Enigmas.

Jens P Andersen1, Anna L Vestergaard1, Stine A Mikkelsen1

  • 1Department of Biomedicine, Aarhus University Aarhus, Denmark.

Frontiers in Physiology
|July 27, 2016
PubMed
Summary

P4-ATPases flip phospholipids across membranes, maintaining lipid asymmetry crucial for cell functions. Their mechanism resembles ion pumps, with a hydrophobic pathway and a mobile isoleucine residue facilitating lipid transport.

Keywords:
ATP8A2CDC50P-type ATPasesP4-ATPasesflippasesmembrane asymmetryphospholipid transport

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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • P4-ATPases are P-type ATPases that actively transport phospholipids, establishing membrane lipid asymmetry.
  • This asymmetry is vital for cellular processes including signaling, vesicle trafficking, and homeostasis.
  • Defects in P4-ATPases like ATP8A2 and ATP8B1 are linked to severe human genetic disorders.

Purpose of the Study:

  • To review the mechanistic insights into phospholipid translocation by P4-ATPases.
  • To highlight the structural and functional properties of mammalian and yeast P4-ATPases.
  • To explore the similarities between P4-ATPase and ion pump mechanisms.

Main Methods:

  • Review of recent studies on P4-ATPase structure and function.
  • Analysis of proposed phospholipid translocation pathways.
  • Comparison with established mechanisms of ion-transporting ATPases.

Main Results:

  • P4-ATPases translocate phospholipids via a phosphorylated intermediate and dephosphorylation activated by the lipid substrate.
  • A peripheral hydrophobic gate pathway involving transmembrane helices M1, M3, M4, and M6 facilitates translocation.
  • An isoleucine residue, analogous to glutamate in ion pumps, drives phospholipid movement.

Conclusions:

  • The P4-ATPase mechanism shares similarities with ion pumps, utilizing a pump-rod-like movement for translocation.
  • The accessory subunit CDC50 may assist in lipid substrate binding at the pathway entrance.
  • Understanding mammalian and yeast P4-ATPases offers insights applicable to other organisms.