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 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 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 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...
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...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
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

Influence of organizational stress on reported depressive symptoms among police.

Occupational medicine (Oxford, England)·2020
Same author

The Impact of Acute Stress Physiology on Skilled Motor Performance: Implications for Policing.

Frontiers in psychology·2019
Same author

Genetic suppression of agrin reduces mania-like behavior in Na+ , K+ -ATPase α3 mutant mice.

Genes, brain, and behavior·2012
Same author

Decreased neuronal Na+, K+ -ATPase activity in Atp1a3 heterozygous mice increases susceptibility to depression-like endophenotypes by chronic variable stress.

Genes, brain, and behavior·2011
Same author

ATP binding residues of sarcoplasmic reticulum Ca2+-ATPase.

Annals of the New York Academy of Sciences·2003
Same author

Importance of Thr-353 of the conserved phosphorylation loop of the sarcoplasmic reticulum Ca2+-ATPase in MgATP binding and catalytic activity.

The Journal of biological chemistry·2001
Same journal

Artificial Intelligence in Echocardiography for Valvular Heart Disease.

Trends in cardiovascular medicine·2026
Same journal

Inflammation as a Fulcrum in Cardiovascular Disease: The Evolving Case for High-Sensitivity C-Reactive Protein.

Trends in cardiovascular medicine·2026
Same journal

Comment on "advancing personalised care in atrial fibrillation and stroke: The potential impact of AI from prevention to rehabilitation".

Trends in cardiovascular medicine·2026
Same journal

Response to: Comment on "Advancing personalised care in atrial fibrillation and stroke: The potential impact of AI from prevention to rehabilitation" (TCM-D-26-00198).

Trends in cardiovascular medicine·2026
Same journal

High-sensitivity C-reactive protein as a prognostic biomarker in cardiovascular diseases: implications for atherosclerosis, chronic kidney disease, and heart failure - a review.

Trends in cardiovascular medicine·2026
Same journal

The cost of false dichotomies in a dynamic disease.

Trends in cardiovascular medicine·2026
See all related articles

Related Experiment Video

Updated: Jun 5, 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

Mutagenesis of Sarcoplasmic Reticulum Ca(2+)-ATPase.

J P Andersen1, B Vilsen

  • 1Department of Physiology, University of Aarhus, Aarhus C, Denmark.

Trends in Cardiovascular Medicine
|January 18, 2011
PubMed
Summary
This summary is machine-generated.

Calcium ATPases in muscle cells use ATP energy for calcium transport. Mutagenesis studies reveal key protein regions and amino acids involved in calcium binding, translocation, and regulation by phospholamban.

More Related Videos

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
12:26

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability

Published on: June 2, 2023

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

Related Experiment Videos

Last Updated: Jun 5, 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

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
12:26

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability

Published on: June 2, 2023

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

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Muscle Physiology

Background:

  • Sarco(endo)plasmic reticulum Ca(2+)-ATPases (SERCA) are crucial for muscle contraction and relaxation by actively transporting calcium ions.
  • Understanding SERCA function is vital for addressing muscle-related disorders and cardiac conditions.

Purpose of the Study:

  • To elucidate the structure-function relationships of Ca(2+)-ATPases using site-directed mutagenesis.
  • To identify specific protein domains and amino acid residues critical for calcium ion binding, occlusion, and translocation.
  • To investigate the role of intramolecular signaling in energy transduction and the interaction with phospholamban.

Main Methods:

  • Site-directed mutagenesis was employed to alter specific amino acid residues within the Ca(2+)-ATPase.
  • Functional assays were performed to assess the impact of mutations on calcium ion binding and transport.
  • Investigated the interaction between cardiac Ca(2+)-ATPase and phospholamban.

Main Results:

  • Identified key protein domains and single amino acid residues essential for calcium ion binding and occlusion during translocation.
  • Discovered amino acid residues critical for energy-transducing intramolecular signaling linking ATP hydrolysis to calcium site rearrangements.
  • Elucidated the interaction mechanism between cardiac sarcoplasmic reticulum Ca(2+)-ATPase and phospholamban, explaining beta-agonist mediated activation.

Conclusions:

  • Site-directed mutagenesis is a powerful tool for dissecting Ca(2+)-ATPase structure-function relationships.
  • Specific residues and domains within Ca(2+)-ATPase are critical for calcium transport and energy transduction.
  • The interaction with phospholamban provides insights into the regulation of cardiac calcium cycling.