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Related Concept Videos

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...
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...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
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 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...

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Related Experiment Video

Updated: May 31, 2026

Ex Vivo Imaging of Cell-specific Calcium Signaling at the Tripartite Synapse of the Mouse Diaphragm
08:42

Ex Vivo Imaging of Cell-specific Calcium Signaling at the Tripartite Synapse of the Mouse Diaphragm

Published on: October 4, 2018

Motion of the Ca2+-pump captured.

Masatoshi Yokokawa1, Kunio Takeyasu

  • 1Kyoto University Graduate School of Biostudies, Kyoto, Japan. yokokawa@ims.tsukuba.ac.jp

The FEBS Journal
|June 29, 2011
PubMed
Summary

Researchers visualized the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) using atomic force microscopy. SERCA

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Ion pumps, like ATP synthetase and Ca(2+)-ATPase, are crucial for cellular functions.
  • Previous studies provided static crystal structures of ion pumps, limiting dynamic mechanism insights.
  • Understanding sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) dynamics is key to calcium transport mechanisms.

Purpose of the Study:

  • To visualize real-time conformational changes of the SERCA ion pump at the single-molecule level.
  • To investigate the dynamic mechanism of SERCA in response to ATP and Ca(2+) concentrations.
  • To compare the observed mechanism with the established Albers-Post scheme.

Main Methods:

  • Fast-scanning atomic force microscopy (AFM) was employed to observe individual SERCA molecules.

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Imaging Ca2+ Signals in Small Pulmonary Veins at Physiological Intraluminal Pressures

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Imaging Local Ca2+ Signals in Cultured Mammalian Cells
09:30

Imaging Local Ca2+ Signals in Cultured Mammalian Cells

Published on: March 3, 2015

Related Experiment Videos

Last Updated: May 31, 2026

Ex Vivo Imaging of Cell-specific Calcium Signaling at the Tripartite Synapse of the Mouse Diaphragm
08:42

Ex Vivo Imaging of Cell-specific Calcium Signaling at the Tripartite Synapse of the Mouse Diaphragm

Published on: October 4, 2018

Imaging Ca2+ Signals in Small Pulmonary Veins at Physiological Intraluminal Pressures
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Imaging Ca2+ Signals in Small Pulmonary Veins at Physiological Intraluminal Pressures

Published on: March 21, 2025

Imaging Local Ca2+ Signals in Cultured Mammalian Cells
09:30

Imaging Local Ca2+ Signals in Cultured Mammalian Cells

Published on: March 3, 2015

  • Real-time imaging allowed visualization of conformational dynamics.
  • Experiments were conducted under varying concentrations of ATP and Ca(2+), and with a specific inhibitor.

    • Main Results:

    • SERCA exhibited up-down structural changes consistent with the Albers-Post scheme under specific conditions.
    • These conformational changes were sensitive to ATP and Ca(2+) concentrations.
    • At physiological ATP concentrations, the characteristic up-down motion of SERCA was completely abolished.

    Conclusions:

    • SERCA's catalytic pathway differs from the standard Albers-Post scheme under physiological conditions.
    • The ion pump does not appear to transit through its shortest structural state during normal function.
    • These findings provide new insights into the dynamic mechanism of ion transport in SERCA.