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Related Concept Videos

ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

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 are...
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

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...
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...
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...

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Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays
12:25

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

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Conservation of copper-transporting P(IB)-type ATPase function.

Adam Southon1, Nickless Palstra, Nicholas Veldhuis

  • 1Department of Genetics, The University of Melbourne, Melbourne, VIC 3010, Australia.

Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
|April 8, 2010
PubMed
Summary
This summary is machine-generated.

The single Drosophila melanogaster copper-transporting ATPase, DmATP7, functionally compensates for the absence of mammalian ATP7A. DmATP7 exhibits conserved trafficking motifs, correcting copper homeostasis defects and phenocopying ATP7A function.

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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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Last Updated: Jun 14, 2026

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays
12:25

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

Published on: September 28, 2018

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

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14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Area of Science:

  • Biochemistry
  • Cell Biology
  • Genetics

Background:

  • Copper-transporting P(IB)-type ATPases (ATP7A and ATP7B) are crucial for copper homeostasis in mammals, regulating copper trafficking from the trans-Golgi Network to the plasma membrane.
  • In polarized cells, ATP7A and ATP7B exhibit distinct apical and basolateral membrane targeting, respectively.
  • Vertebrate evolution involved a gene duplication of these ATPases, unlike unicellular eukaryotes and invertebrates with a single orthologue.

Purpose of the Study:

  • To investigate the conserved function and localization of DmATP7, the sole orthologue of ATP7A/B in Drosophila melanogaster.
  • To explore the functional conservation of P(IB)-type ATPase mechanisms across distant species.
  • To determine if DmATP7 can rescue copper transport defects in mammalian cells.

Main Methods:

  • Comparative genomic analysis of ATP7A/B targeting motifs and DmATP7.
  • Expression of DmATP7 in cultured mammalian cells, including fibroblasts from a Menkes disease patient (ATP7A null).
  • Localization studies in polarized Madin-Darby Canine Kidney cells under varying copper conditions.

Main Results:

  • DmATP7 possesses conserved basolateral targeting motifs similar to ATP7A, but not ATP7B.
  • DmATP7 expression rescued the copper hyper-accumulation phenotype in ATP7A-deficient Menkes disease fibroblasts.
  • DmATP7 trafficked to the plasma membrane and effluxed copper under high copper conditions, mimicking ATP7A.
  • In polarized cells, DmATP7 localized to the basolateral membrane upon copper elevation, similar to ATP7A.

Conclusions:

  • DmATP7 functionally compensates for ATP7A, demonstrating conserved roles in copper transport and homeostasis.
  • Key trafficking motifs for basolateral targeting are conserved between DmATP7 and ATP7A despite evolutionary distance.
  • DmATP7 serves as a valuable model for studying conserved P(IB)-type ATPase mechanisms and copper metabolism.