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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.
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Non-Canonical Wnt Signaling Pathways

Wnt is a zygotic effect gene that is expressed during very early embryonic development. It regulates various processes in animals starting from early development through the adult stage, such as organogenesis in the embryo and maintenance of neuronal and blood stem cells. Wnt proteins can induce a wide variety of intracellular pathways depending upon the specific abilities of different Wnt ligands to form a complex with shared and cognate receptors in the presence of different co-receptors. The...
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The primary cilium, made up of microtubules, acts as antennae on the cell surfaces for relaying external stimuli into the cells. These fine hair-like structures are present, generally one per cell. These are non-motile cilia in a 9+0 microtubules arrangement, where the central pair of microtubules are absent. The primary cilia arise from the basal body embedded in the cell membrane. Intraflagellar transport (IFT) carries requisite proteins from the cytoplasm to the cilium because the primary...
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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

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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...
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Contact-dependent Signaling

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Gap Junctions
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Immunostaining Phospho-epitopes in Ciliated Organs of Whole Mount Zebrafish Embryos
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Ca2+ signalling early in evolution--all but primitive.

Helmut Plattner1, Alexei Verkhratsky

  • 1Faculty of Biology, University of Konstanz, 78457 Konstanz, Germany. helmut.plattner@uni-konstanz.de

Journal of Cell Science
|June 5, 2013
PubMed
Summary

Calcium (Ca2+) acts as a crucial second messenger. This study identifies 34 distinct Ca2+-release channels in Paramecium, revealing diverse evolutionary pathways for cellular signaling.

Keywords:
Ca2+Ca2+-release channelsCalciumProtistProtozoa

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Area of Science:

  • Cellular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Calcium (Ca2+) is a vital second messenger regulating diverse cellular functions in eukaryotes.
  • Inositol 1,4,5-trisphosphate receptors (InsP3R) and ryanodine receptors (RyR) are key Ca2+-release channels in mammals.
  • Ca2+-release channels in unicellular organisms and plants are less understood.

Purpose of the Study:

  • To investigate the evolutionary origins and diversity of Ca2+-release channels in protozoa.
  • To characterize the molecular and functional aspects of Ca2+-release channels in Paramecium tetraurelia.
  • To map the evolutionary trajectories of Ca2+-release machinery in early eukaryotes.

Main Methods:

  • Bioinformatic analysis of Ca2+-release channel genes in Paramecium tetraurelia.
  • Domain structure, pore, selectivity filter, and activation mechanism analysis.
  • Localization and gene silencing experiments to determine channel function.

Main Results:

  • Identified 34 distinct Ca2+-release channels in Paramecium, categorized into six subfamilies.
  • Some channels are identified as InsP3R or RyR homologs, while others possess mixed characteristics.
  • Demonstrated distinct localization, activation, and functional roles for these diverse channels.

Conclusions:

  • Paramecium tetraurelia possesses a complex and diverse array of Ca2+-release channels, reflecting early evolutionary adaptations.
  • Detailed domain and functional analyses are crucial for understanding the evolution of Ca2+-release channels in unicellular organisms.
  • This study provides insights into the early evolution of intracellular calcium signaling pathways.