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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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,...
Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
Types of Signaling Molecules01:32

Types of Signaling Molecules

In multicellular organisms, many molecules transmit signals between cells to pass information. These signals vary in complexity and include small peptides, nucleotides, steroids, fatty acid derivatives, and dissolved gases such as nitric oxide. Some signaling molecules diffuse through the plasma membrane to act locally between neighboring cells or travel long distances. Others remain attached to the cell surface, transmitting information to other cells only when they make contact. In some...
Nitric Oxide Signaling Pathway01:28

Nitric Oxide Signaling Pathway

Nitric oxide (NO), an inorganic gas, acts as a potent second messenger in most animal and plant tissues. NO diffuses out of the cells that produce it and enters the neighboring cells to generate a downstream response. NO synthase (NOS) catalyzes NO production by the deamination of the amino acid arginine. There are three isoforms of NOS. Endothelial cells have endothelial NOS (eNOS), nerve and muscle cells have neuronal NOS (nNOS), and macrophages produce inducible NOS (iNOS) upon exposure to...

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Related Experiment Video

Updated: Jul 13, 2026

Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators
11:33

Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators

Published on: March 22, 2019

Shooting blanks: Ca2+-free signaling.

Brian D Sykes

    Structure (London, England : 1993)
    |July 20, 2007
    PubMed
    Summary

    Insect flight muscles achieve high frequencies due to a unique Ca2+ binding protein. This protein

    Area of Science:

    • Muscle physiology
    • Biochemistry
    • Structural biology

    Background:

    • Insect flight muscles exhibit remarkable high-frequency oscillatory contractions.
    • Understanding the molecular mechanisms behind this capability is crucial for biomechanics.

    Discussion:

    • De Nicola et al. elucidate the structure of a key Ca2+ binding protein.
    • This protein regulates asynchronous muscle contraction in insects.

    Key Insights:

    • The protein's structure provides insights into the mechanism of stretch activation.
    • This finding advances our understanding of muscle function at high frequencies.

    Outlook:

    • Further research can explore therapeutic applications for muscle disorders.

    More Related Videos

    Imaging Local Ca2+ Signals in Cultured Mammalian Cells
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    Imaging Local Ca2+ Signals in Cultured Mammalian Cells

    Published on: March 3, 2015

    Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
    13:40

    Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

    Published on: July 7, 2011

    Related Experiment Videos

    Last Updated: Jul 13, 2026

    Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators
    11:33

    Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators

    Published on: March 22, 2019

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

    Imaging Local Ca2+ Signals in Cultured Mammalian Cells

    Published on: March 3, 2015

    Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
    13:40

    Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

    Published on: July 7, 2011

  • Comparative studies may reveal conserved mechanisms across different species.