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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

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...
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

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...
Primary Active Transport01:29

Primary Active Transport

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 not...
Primary Active Transport01:47

Primary Active Transport

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 they...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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 ATP...
Active Transport01:14

Active Transport

Active transport is a critical biological process that allows cells to move solutes against an electrochemical gradient. This process requires direct energy input and is characterized by its selectivity, saturability, and susceptibility to competitive inhibition.
Primary active transporters, like Na+, K+ and -ATPase, directly utilize ATP to move ions across the membrane. These transporters play significant roles in various physiological processes. For instance, Na+, K+ and -ATPase maintain...

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Related Experiment Video

Updated: Jul 11, 2026

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

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

Published on: February 19, 2013

Structural and functional interactions between FXYD5 and the Na+-K+-ATPase.

Irina Lubarski1, Steven J D Karlish, Haim Garty

  • 1Dept. of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.

American Journal of Physiology. Renal Physiology
|September 21, 2007
PubMed
Summary

The transmembrane domain of FXYD5 is crucial for its interaction with the Na(+)-K(+)-ATPase pump, enhancing its function. Researchers also identified a splice variant and glycosylation of FXYD5, suggesting broader roles.

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Last Updated: Jul 11, 2026

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Physiology

Background:

  • FXYD5 is a kidney tubule regulator of the Na(+)-K(+)-ATPase.
  • Previous work showed FXYD5 interacts with Na(+)-K(+)-ATPase subunits, increasing its V(max).

Purpose of the Study:

  • Further characterize FXYD5's structural interactions and structure-function relationships.
  • Identify key regions and amino acids involved in FXYD5-Na(+)-K(+)-ATPase interaction.
  • Investigate potential alternative functional mechanisms of FXYD5.

Main Methods:

  • Xenopus laevis oocyte expression system.
  • Construction and expression of FXYD5/FXYD4 chimeras.
  • Wheat germ agglutinin binding assays.

Main Results:

  • The transmembrane domain of FXYD5 mediates high-affinity association with Na(+)-K(+)-ATPase and increases V(max).
  • Specific amino acids involved in FXYD5-alpha-subunit interaction were identified.
  • A splice variant of FXYD5 with a 10-amino acid extension at the COOH terminus was found.
  • FXYD5 is glycosylated, but this does not significantly alter its size in native epithelia or oocytes.

Conclusions:

  • The transmembrane domain is critical for FXYD5's interaction with and functional modulation of Na(+)-K(+)-ATPase.
  • FXYD proteins likely share similar interaction mechanisms via their transmembrane domains.
  • The FXYD5 splice variant and glycosylation suggest potential additional, non-transmembrane-mediated functions.