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

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.1K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.1K
Structure of Cadherins01:25

Structure of Cadherins

3.3K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
3.3K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.7K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
5.7K
Diversity in Cell Signaling Responses01:22

Diversity in Cell Signaling Responses

6.3K
The physiological function of a cell and cellular communication are outcomes of a range of extrinsic signals, intracellular signaling pathways, and cellular responses. No two cell types express the same repertoire of signaling components. Receptors are highly selective for their cognate ligands, but once activated, they can alter multiple cellular processes such as DNA transcription, protein synthesis, and metabolic activity. 
Graded and Abrupt Responses
Some signaling systems generate...
6.3K
Skeleton and Calcium Homeostasis01:21

Skeleton and Calcium Homeostasis

4.4K
Calcium is not only the most abundant mineral in bone but also the most abundant mineral in the human body. Calcium ions are needed for bone mineralization, tooth health, heart rate regulation and strength of contraction, blood coagulation, the contraction of smooth and skeletal muscle cells, and the regulation of nerve impulse conduction. The average calcium level in the blood is about 10 mg/dL. When the body cannot maintain this level, a person will experience hypo or hypercalcemia.
4.4K
Cell-surface Signaling01:21

Cell-surface Signaling

51.4K
Hormones—or any molecule that binds to a receptor, known as a ligand—that are lipid-insoluble (water-soluble) are not able to diffuse across the cell membrane. In order to be able to affect a cell without entering it, these hormones bind to receptors on the cell membrane. When a first messenger, a hormone, binds to a receptor, a signal cascade is set off, causing second messengers, proteins inside the cell, to become activated, resulting in downstream effects.
51.4K

You might also read

Related Articles

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

Sort by
Same author

Cardiac ventricular Kir6.1 ATP-sensitive potassium channels: an overlooked effector of cardioprotection.

Frontiers in physiology·2026
Same author

Calmodulin D133H Disrupts Ca<sub>v</sub>1.2 and K<sub>v</sub>7.1 Regulation to Prolong Cardiac Action Potentials in Long QT Syndrome.

Cells·2025
Same author

Preeclamptic Placental CD19+ B Cells Are Causal to Hypertension During Pregnancy.

Hypertension (Dallas, Tex. : 1979)·2025
Same author

Arrhythmogenic calmodulin variants D131E and Q135P disrupt interaction with the L-type voltage-gated Ca<sup>2+</sup> channel (Ca<sub>v</sub>1.2) and reduce Ca<sup>2+</sup>-dependent inactivation.

Acta physiologica (Oxford, England)·2025
Same author

Hypertension and Cognitive Dysfunction in a Pregnant Rat Model of PE; a Role for CD4+ T Cells.

American journal of reproductive immunology (New York, N.Y. : 1989)·2024
Same author

Identification and characterisation of functional K<sub>ir</sub>6.1-containing ATP-sensitive potassium channels in the cardiac ventricular sarcolemmal membrane.

British journal of pharmacology·2024

Related Experiment Video

Updated: May 28, 2025

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED
09:32

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED

Published on: May 7, 2013

19.1K

Structure-Function Diversity of Calcium-Binding Proteins (CaBPs): Key Roles in Cell Signalling and Disease.

Vanessa S Morris1, Ella M B Richards1, Rachael Morris1

  • 1Department of Biochemistry, Cell and Systems Biology, Institute of Systems, Molecular and Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 3BX, UK.

Cells
|February 12, 2025
PubMed
Summary

Calcium (Ca2+) signaling relies on Ca2+-binding proteins (CaBPs). This review analyzes CaBP structure-function, comparing family members and highlighting knowledge gaps and disease-related mutations for CaBP research.

Keywords:
calcium channelscalcium signallingcalcium-binding proteinsinteractionsion channelsstructural biology

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

14.8K
Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

25.3K

Related Experiment Videos

Last Updated: May 28, 2025

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED
09:32

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED

Published on: May 7, 2013

19.1K
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

14.8K
Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

25.3K

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Calcium (Ca2+) signaling is a fundamental cellular process vital for numerous physiological functions.
  • Calcium-binding proteins (CaBPs) regulate Ca2+ signaling, with six family members (CaBP1-5, CaBP7, CaBP8) exhibiting distinct characteristics.
  • CaBPs share similarities with calmodulin (CaM), another key Ca2+-binding protein.

Purpose of the Study:

  • To provide a comprehensive structure-function analysis of the CaBP family.
  • To highlight similarities and differences within the CaBP family and compared to CaM.
  • To identify knowledge gaps and examine the impact of pathogenic mutations in CaBPs.

Main Methods:

  • Literature review and analysis of existing CaBP research.
  • Comparative structural and functional analysis of CaBP family members.
  • Examination of reported pathogenic mutations and their functional consequences.

Main Results:

  • CaBP1-5 share conserved structural and interaction properties.
  • CaBP7 and CaBP8 form a distinct subfamily with unique features.
  • Significant knowledge gaps exist for certain CaBP members, and pathogenic mutations impact protein function.

Conclusions:

  • Understanding CaBP structure-function relationships is crucial for elucidating Ca2+ signaling pathways.
  • Further research is needed to address knowledge gaps and explore therapeutic strategies for CaBP-associated disorders.
  • CaBP mutations underscore their importance in human health and disease.