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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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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.
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Gap Junctions01:37

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Multicellular organisms employ a variety of ways for cells to communicate with each other. Gap junctions are specialized proteins that form pores between neighboring cells in animals, connecting the cytoplasm between the two, and allowing for the exchange of molecules and ions. They are found in a wide range of invertebrate and vertebrate species, mediate numerous functions including cell differentiation and development, and are associated with numerous human diseases, including cardiac and...
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Gap Junctions01:27

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The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
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Feedback Regulation of Calcium Concentration01:27

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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.
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Contact-dependent Signaling01:19

Contact-dependent Signaling

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Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
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Overview of Cell-Cell Junctions01:14

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The complex three-dimensional arrangement of cells in any multicellular organism is defined and maintained by interactions of cells with each other and the extracellular matrix. Cell-cell junctions are specialized structures where the multi-protein complexes on one cell interact with the multi-protein complexes on another  cell. These cell junctions are classified  into three main types based on their function — occluding, anchoring, and gap junctions.
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Pull-down of Calmodulin-binding Proteins
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Gap junction regulation by calmodulin.

Juan Zou1, Mani Salarian1, Yanyi Chen1

  • 1Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, United States.

FEBS Letters
|January 21, 2014
PubMed
Summary
This summary is machine-generated.

Calmodulin (CaM) inhibits cellular communication via gap junction channels. This Ca(2+)-dependent regulation is crucial for hearing, vision, and heart function.

Keywords:
Ca(2+)Calmodulin bindingConnexinGap junction regulation

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Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Physiology

Background:

  • Gap junction channels mediate direct cell-to-cell communication.
  • Intracellular calcium (Ca2+) levels regulate various cellular processes, including hearing, lens transparency, and cardiac function.
  • Calmodulin (CaM) is a key calcium-binding protein involved in cellular signaling.

Purpose of the Study:

  • To investigate the direct role of CaM in regulating connexin-based gap junction channels.
  • To identify and characterize Ca2+-dependent CaM binding sites on connexin proteins.
  • To determine the binding affinities of CaM to different connexin subfamilies.

Main Methods:

  • Utilized peptide models representing putative CaM binding sites within connexin intracellular domains.
  • Employed biochemical assays to measure Ca2+-dependent CaM binding affinities.
  • Focused on connexin subfamilies to understand diverse regulatory mechanisms.

Main Results:

  • Demonstrated that intracellular Ca2+-activated CaM inhibits gap junction channel function across a broad range of Ca2+ concentrations.
  • Identified specific Ca2+-dependent CaM binding sites on connexin peptides.
  • Quantified CaM binding affinities for peptides from various connexin subfamilies, revealing differential regulation.

Conclusions:

  • CaM directly binds to and inhibits gap junction channels in a Ca2+-dependent manner.
  • This interaction is a critical regulatory mechanism for cell-to-cell communication in vital physiological processes.
  • Understanding these interactions provides insights into connexin channel function and potential therapeutic targets.