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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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Phosphoinositides and PIPs01:42

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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 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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ATP Synthase: Structure01:18

ATP Synthase: Structure

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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 Synthase: Mechanism01:48

ATP Synthase: Mechanism

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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Related Experiment Video

Updated: Apr 23, 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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Substrate trajectory through phospholipid-transporting P4-ATPases.

Patrick Williamson1

  • 1*Department of Biology and Program in Biochemistry and Biophysics, Amherst College, Amherst, MA 01002, U.S.A.

Biochemical Society Transactions
|September 19, 2014
PubMed
Summary
This summary is machine-generated.

Generating lipid asymmetry in cell membranes requires active transport. P-type ATPases use ATP hydrolysis to move lipids, but the exact path phospholipids take through these enzymes is still under investigation, with three models proposed.

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Related Experiment Videos

Last Updated: Apr 23, 2026

A Fluorescence-based Assay of Phospholipid Scramblase Activity
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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Membrane Biophysics

Background:

  • Cell membranes exhibit lipid compositional heterogeneity, with distinct lipid distributions between leaflets.
  • Transbilayer movement of certain lipids is restricted by high activation energy barriers.
  • Eukaryotic evolution involved developing mechanisms for generating lipid asymmetry far from equilibrium using ATP.

Purpose of the Study:

  • To investigate the mechanism of P-type ATPases in creating transbilayer lipid asymmetry.
  • To elucidate the trajectory of phospholipid substrates through P-type ATPases.

Main Methods:

  • Analysis of ATP hydrolysis by P-type ATPases.
  • Mutation and activity measurements to probe enzyme mechanisms.
  • Comparison with known atomic structures of related enzymes.

Main Results:

  • The mechanism of ATP hydrolysis by P-type ATPases is understood.
  • The precise trajectory of phospholipid substrates remains an active area of research.
  • Three distinct models for phospholipid substrate trajectory are currently supported by experimental data and structural analogies.

Conclusions:

  • P-type ATPases are crucial for generating and maintaining lipid asymmetry in eukaryotic cells.
  • Understanding the phospholipid substrate trajectory is key to fully elucidating P-type ATPase function.
  • Ongoing research utilizing biochemical and structural approaches aims to resolve the proposed models.