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Related Concept Videos

ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

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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.
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Regulation of Sodium and Potassium01:26

Regulation of Sodium and Potassium

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The regulation of sodium and potassium ion concentrations in the human body is a complex process governed primarily by hormones such as aldosterone, antidiuretic hormone (ADH), and atrial natriuretic peptide (ANP).
Sodium Regulation
Sodium ions make up approximately 90% of extracellular cations, with a normal blood plasma concentration of 136–148 mEq/L. A decrease in blood volume and pressure triggers the release of renin from granular cells in the juxtaglomerular complex (JGC), primarily...
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ATP Driven Pumps I: An Overview01:27

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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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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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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

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FXYD protein isoforms differentially modulate human Na/K pump function.

Dylan J Meyer1, Sharan Bijlani1, Marilina de Sautu1

  • 1Department of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock TX.

The Journal of General Physiology
|November 24, 2020
PubMed
Summary
This summary is machine-generated.

Five FXYD proteins regulate the sodium-potassium pump (Na/K pump), affecting ion affinity and turnover. FXYD1 and FXYD6 also significantly reduce Na/K pump surface expression, impacting cellular function.

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Area of Science:

  • Biochemistry
  • Cellular Physiology
  • Molecular Biology

Background:

  • The sodium-potassium pump (Na/K pump) is crucial for maintaining cellular electrochemical gradients.
  • Regulation of the Na/K pump is essential for cellular function, impacting electrical signaling and transport.
  • FXYD proteins are known regulators of the Na/K pump, with specific tissue localizations.

Purpose of the Study:

  • To investigate the regulatory mechanisms of the human Na/K pump α1β1 isoform by five human FXYD proteins.
  • To elucidate how FXYD proteins influence the Na/K pump's ion affinity, conformational states, and overall function.
  • To determine the impact of FXYD proteins on Na/K pump surface expression and trafficking.

Main Methods:

  • Expression of human Na/K pump α1β1 and FXYD isoforms in Xenopus oocytes.
  • Electrophysiological recordings using two-electrode voltage clamp and patch clamp techniques.
  • Analysis of partial reactions to assess ion binding and conformational changes.

Main Results:

  • FXYD proteins alter the equilibrium between E1P(3Na) and E2P conformations, modifying apparent Na+ affinity.
  • FXYD6 specifically accelerates Na+-deocclusion and pump-turnover rates.
  • All FXYD isoforms affect intracellular Na+ affinity and alter pump selectivity for intracellular ions.
  • FXYD1 and FXYD6 drastically reduce Na/K pump surface expression, suggesting a role in pump trafficking regulation.

Conclusions:

  • FXYD proteins are key regulators of Na/K pump function, influencing ion binding, kinetics, and conformational dynamics.
  • FXYD proteins modulate the Na/K pump's interaction with both intracellular and extracellular ions.
  • FXYD1 and FXYD6 play a significant role in regulating Na/K pump trafficking and surface expression, with implications for cellular homeostasis.