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Related Concept Videos

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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The resting membrane potential of a neuron (-70mV) is sustained due to the selective ion permeability of the membrane. At the resting potential, the membrane is slightly permeable to ions like sodium (Na+) and chloride (Cl−) and highly permeable to potassium ions (K+). Differences in the ions' concentration inside the cell compared to the outside are maintained by membrane transport proteins like channels and pumps.
At rest, the K+ is the main ion that moves across the membrane...
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Pore transport and ion-pair formation are critical mechanisms for the absorption and distribution of drugs in the body.
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Primary Active Transport01:29

Primary Active Transport

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In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would...
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Primary Active Transport01:47

Primary Active Transport

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In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps that are embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction...
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The interionic forces of the strong electrolytes depend on the solvent's dielectric constant, which is the ability of a solvent to store electrical energy, based on its polarizability. and the solution's concentration. In high-dielectric solvents and in dilute solutions, weak electrostatic forces keep ions apart. However, in low-dielectric solvents or concentrated solutions, stronger interionic forces may cause ions to pair up as ionic doublets despite being fully ionized. The theory of strong...
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Evolutionary Prevalence of the Electrostatic Switch Mechanism in P-type ATPases.

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Electrostatic Interaction as a Key Modulator of Na<sup>+</sup>,K<sup>+</sup>-ATPase Function.

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IUPAB Focused-Meeting on P-Type ATPases: 17th International Conference on P-type ATPases in Health and Disease.

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Swartkrans <i>Paranthropus</i> and Sterkfontein <i>Australopithecus</i> from southern Africa had different locomotor repertoires.

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Correction: Cholesterol depletion inhibits Na+,K+-ATPase activity in a near-native membrane environment.

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Corrigendum to "Interaction of N-terminal peptide analogues of the Na+,K+-ATPase with membranes" [BBA Biomembr. 1860 (6) (2018) 1282-1291].

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Dipole-Potential-Mediated Effects on Ion Pump Kinetics.

Ronald J Clarke1

  • 1School of Chemistry, University of Sydney, Sydney, Australia.

Biophysical Journal
|October 22, 2015
PubMed
Summary

Membrane composition influences P-type ATPase ion transport kinetics by altering lipid dipole potential. This mechanism explains how membrane lipids affect protein conformational changes and ion pump activity.

Area of Science:

  • Biochemistry
  • Membrane Biophysics
  • Structural Biology

Background:

  • P-type ATPase ion transport kinetics are sensitive to membrane composition, including phospholipids, cholesterol, and lipid-bound anions.
  • Membrane components can alter the lipid head-group region's dipole potential.
  • Ion pump activity perturbs the surrounding membrane environment.

Purpose of the Study:

  • To propose a mechanism explaining how membrane dipole potential modifiers affect P-type ATPase conformational kinetics.
  • To elucidate the role of lipid-protein interactions in regulating ion pump function.

Main Methods:

  • Theoretical mechanism based on hydrophobic matching and lipid packing density changes.
  • Analysis of how conformational changes alter protein hydrophobic thickness.

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  • Postulation of lipid dipole potential modulation by protein activity.

    • Main Results:

    • Dipole potential modifiers preferentially stabilize or destabilize occluded/nonoccluded protein states.
    • Changes in lipid packing density alter local lipid dipole potential.
    • This leads to altered forward and backward rate constants for conformational transitions.

    Conclusions:

    • The proposed mechanism links lipid composition-dependent kinetics to changes in protein hydrophobic thickness and local lipid dipole potential.
    • This model can explain the influence of membrane properties on the kinetics of various membrane proteins with changing cross-sectional areas.