Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
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...
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...
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...
Relaxation of Skeletal Muscles01:29

Relaxation of Skeletal Muscles

The period of muscle contraction primarily influences the duration of stimulation at the neuromuscular junction (NMJ), the presence of free calcium ions in the sarcoplasm, and the availability of energy or ATP to support contractions.
When an action potential reaches the axon terminal, it depolarizes the membrane and opens voltage-gated sodium channels. Sodium ions enter the cell, further depolarizing the presynaptic membrane. This depolarization causes voltage-gated calcium channels to open.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Distinct transport cycle and lipid regulation of a Mg<sup>2+</sup>-transporting P-type ATPase, MgtA.

Research square·2026
Same author

Kell-Score-A web resource for estimating the immunogenicity of novel Kell blood group variants.

British journal of haematology·2026
Same author

Structure of α-Synuclein Bound to Polystyrene Surfaces Probed by Experimental and Theoretical Sum Frequency Generation Spectroscopy.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

<i>Grin2b</i> 3'UTR is necessary for synaptic plasticity and spatial learning.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Derivatization of Bufadienolides at Carbon-3 of the Steroid Core and Their Consequences for the Interaction with Na<sup>+</sup>,K<sup>+</sup>-ATPase.

International journal of molecular sciences·2025
Same author

Dynamics and structural features of the eEF1A1 and eEF1A2 paralogs.

Nucleic acids research·2025

Related Experiment Video

Updated: May 14, 2026

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle
08:37

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

Published on: March 21, 2025

Ion pathways in the sarcoplasmic reticulum Ca2+-ATPase.

Maike Bublitz1, Maria Musgaard, Hanne Poulsen

  • 1Centre for Membrane Pumps in Cells and Disease (PUMPkin), Aarhus University, DK-8000 Aarhus C, Denmark.

The Journal of Biological Chemistry
|February 13, 2013
PubMed
Summary

The sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA) uses two cytoplasmic pathways for ion exchange. A newly identified C-terminal pathway facilitates proton release in SERCA E2 states.

More Related Videos

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+
12:30

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+

Published on: May 19, 2017

Assessment of Sarcoplasmic Reticulum Calcium Reserve and Intracellular Diastolic Calcium Removal in Isolated Ventricular Cardiomyocytes
11:00

Assessment of Sarcoplasmic Reticulum Calcium Reserve and Intracellular Diastolic Calcium Removal in Isolated Ventricular Cardiomyocytes

Published on: September 18, 2017

Related Experiment Videos

Last Updated: May 14, 2026

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle
08:37

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

Published on: March 21, 2025

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+
12:30

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+

Published on: May 19, 2017

Assessment of Sarcoplasmic Reticulum Calcium Reserve and Intracellular Diastolic Calcium Removal in Isolated Ventricular Cardiomyocytes
11:00

Assessment of Sarcoplasmic Reticulum Calcium Reserve and Intracellular Diastolic Calcium Removal in Isolated Ventricular Cardiomyocytes

Published on: September 18, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA) is a P(II)-type ATPase crucial for muscle contraction and calcium signaling.
  • SERCA actively transports calcium ions (Ca2+) from the cytoplasm into the sarco/endoplasmic reticulum lumen.
  • Understanding SERCA's ion transport mechanism is vital for comprehending cellular calcium homeostasis.

Purpose of the Study:

  • To elucidate the transport pathways for Ca(2+) and H(+) ions across the lipid bilayer mediated by SERCA.
  • To investigate the functional role of a recently identified hydrated pathway in SERCA's C-terminal transmembrane region.
  • To propose a comprehensive model for the ion exchange mechanism in P(II)-ATPases.

Main Methods:

  • Analysis of high-resolution crystal structures of rabbit SERCA1a.
  • Molecular dynamics simulations.
  • Mutational studies.

Main Results:

  • SERCA ion-binding sites are accessible from both the cytoplasm and the ER lumen.
  • A hydrated C-terminal pathway, exclusive to Ca(2+)-free E2 states, facilitates ion release to the cytosol.
  • This pathway shows functional analogy to a similar pathway in the sodium pump.

Conclusions:

  • The C-terminal pathway likely plays a key role in proton release during SERCA's transport cycle.
  • A model involving two concerted cytoplasmic pathways is proposed for P(II)-ATPase ion exchange.
  • This finding enhances our understanding of the intricate mechanisms governing ion transport in ATPases.