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ATP Driven Pumps II: P-type Pumps

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...

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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.
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...

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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 they...

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Transcellular transport of solutes is the movement of substances like monosaccharides and amino acids through polarized cells. This transport mechanism is primarily seen in epithelial and endothelial cells aided by membrane transport proteins such as channels and transporters. The tight junctions between these cells confine the membrane proteins to the two sides of the cell. The epithelial cells have distinct apical and basolateral domains. In contrast, the endothelial cells show the luminal...

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Related Experiment Video

Updated: Jul 10, 2026

Application of Electrophysiology Measurement to Study the Activity of Electro-Neutral Transporters

Application of Electrophysiology Measurement to Study the Activity of Electro-Neutral Transporters

Published on: February 3, 2018

Sodium pump localization in epithelia.

Jason S Bystriansky¹, Jack H Kaplan

¹Department of Biochemistry & Molecular Genetics, University of Illinois at Chicago, Molecular Biology Research Building, 900 S Ashland Avenue, Chicago, IL 60607, USA. jbystria@uic.edu

Journal of Bioenergetics and Biomembranes

|November 1, 2007

Summary

The sodium pump

Area of Science:

Cell Biology
Epithelial Biology
Ion Transport

Background:

Epithelial cells rely on the polarized sodium pump for directional ion and water transport.
Maintaining sodium pump localization to the basolateral surface is crucial for epithelial function.
Mechanisms governing sodium pump targeting and trafficking remain poorly understood.

Purpose of the Study:

To investigate factors regulating sodium pump cellular distribution.
To clarify the role of the sodium pump beta-subunit in epithelial polarity.
To re-evaluate the impact of the beta2 isoform versus growth media components on sodium pump localization.

Main Methods:

Review of existing literature on sodium pump trafficking.
Analysis of studies investigating sodium pump beta-subunit isoforms.

More Related Videos

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Functional Characterization of Na⁺/H⁺ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Published on: March 30, 2015

Related Experiment Videos

Last Updated: Jul 10, 2026

Application of Electrophysiology Measurement to Study the Activity of Electro-Neutral Transporters

Application of Electrophysiology Measurement to Study the Activity of Electro-Neutral Transporters

Published on: February 3, 2018

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Functional Characterization of Na⁺/H⁺ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Published on: March 30, 2015

Examination of experimental data concerning butyrate's effect on epithelial polarity.

Main Results:

Previous findings suggesting beta2 isoform causes apical localization were re-examined.
Apical targeting of the sodium pump in MDCK cells was attributed to butyrate in growth media, not the beta2 isoform.
Butyrate's influence on epithelial sodium pump polarity is a key factor.

Conclusions:

The beta2 isoform is not solely responsible for apical sodium pump localization.
Butyrate in cell culture media can induce aberrant sodium pump polarity.
Further research is needed to elucidate butyrate's precise mechanisms in regulating epithelial sodium pump distribution.