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Aquaporins

Aquaporins

Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.

ATP Driven Pumps III: V-type Pumps

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...

Reabsorption and Secretion in the DCT and Collecting Duct

Reabsorption and Secretion in the DCT and Collecting Duct

The early phase of the DCT manages the reabsorption of approximately 10-15% of filtered water, 5–10% of filtered sodium, and 5–10% of filtered chloride. This process is facilitated by Na+–Cl− symporters in apical membranes and sodium-potassium pumps, as well as Cl− leakage channels in basolateral membranes. The early DCT also stands out as a site where parathyroid hormone (PTH) stimulates calcium reabsorption, depending on the body's requirements.
The distal part of the DCT, along with the...

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...

The ADP/ATP Carrier Protein

The ADP/ATP Carrier Protein

ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...

ATP Driven Pumps I: An Overview

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...

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Related Experiment Video

Updated: Jun 25, 2026

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Published on: December 12, 2025

[Aquaporin-4].

Kazutoshi Tani¹, Yoko Hiroaki, Yoshinori Fujiyoshi

¹Department of Biophysics, Faculty of Science, Kyoto University.

Rinsho Shinkeigaku = Clinical Neurology

|February 10, 2009

Summary

Aquaporin-4 (AQP4) water channels in the brain have a complex structure and function. Palmitoylation impacts AQP4

Area of Science:

Structural biology
Neuroscience
Biophysics

Context:

Aquaporin-4 (AQP4) is a key water channel in the mammalian brain.
AQP4 is implicated in neurological disorders like epilepsy and cerebral edema.
Patient antibodies in multiple sclerosis target AQP4.

Purpose:

Determine the atomic structure of AQP4.
Investigate AQP4's function and membrane interactions.
Understand the role of palmitoylation in AQP4 structure.

Summary:

Electron crystallography revealed AQP4's atomic structure in double-layered crystals.
A 310 helix in extracellular loop C suggests weak adhesive activity between membranes.
Palmitoylation of N-terminal cysteines destabilizes orthogonal arrays on cell membranes.

More Related Videos

Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay

Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay

Published on: April 5, 2019

Visualizing Astrocyte Morphology Using Lucifer Yellow Iontophoresis

Visualizing Astrocyte Morphology Using Lucifer Yellow Iontophoresis

Published on: September 14, 2019

Related Experiment Videos

Last Updated: Jun 25, 2026

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Published on: December 12, 2025

Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay

Human Serum Anti-aquaporin-4 Immunoglobulin G Detection by Cell-based Assay

Published on: April 5, 2019

Visualizing Astrocyte Morphology Using Lucifer Yellow Iontophoresis

Visualizing Astrocyte Morphology Using Lucifer Yellow Iontophoresis

Published on: September 14, 2019

Impact:

Provides insights into AQP4's role in brain water homeostasis.
Correlates structural findings with AQP4's function in glial lamellae.
Suggests a complex regulatory mechanism for brain water content involving AQP4.