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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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NF-κB-dependent Signaling Pathway02:26

NF-κB-dependent Signaling Pathway

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The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
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Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

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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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The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

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Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

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Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
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Related Experiment Video

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Activation and Measurement of NLRP3 Inflammasome Activity Using IL-1β in Human Monocyte-derived Dendritic Cells
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Activation and Measurement of NLRP3 Inflammasome Activity Using IL-1β in Human Monocyte-derived Dendritic Cells

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Interleukin-1β Processing Is Dependent on a Calcium-mediated Interaction with Calmodulin.

Joseph S Ainscough1, G Frank Gerberick2, Ian Kimber3

  • 1From the Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom and joseph.ainscough@postgrad.manchester.ac.uk.

The Journal of Biological Chemistry
|November 13, 2015
PubMed
Summary

Interleukin-1β (IL-1β) secretion requires calcium and calmodulin. This study identifies calmodulin as a key protein interacting with pro-IL-1β, crucial for its release and inflammation initiation.

Keywords:
IL-1IL-1βcalciumcalmodulin (CaM)caspase 1 (CASP1)inflammasome

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Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
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Pull-down of Calmodulin-binding Proteins
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Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
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Pull-down of Calmodulin-binding Proteins
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Pull-down of Calmodulin-binding Proteins

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • Interleukin-1β (IL-1β) secretion is critical for initiating inflammation.
  • IL-1β release requires two signals and involves caspase-1 processing, but the secretion mechanism remains unclear.

Purpose of the Study:

  • To identify novel proteins involved in IL-1β secretion and intracellular processing.
  • To elucidate the mechanism of IL-1β release.

Main Methods:

  • Human proteome microarray screening to identify pro-IL-1β binding proteins.
  • ELISA-based assays to confirm protein interactions and calcium dependency.
  • Small molecule inhibitors to assess the role of calcium and calmodulin in IL-1β secretion in cell models.

Main Results:

  • Calmodulin was identified as a strong binder of pro-IL-1β using a proteome microarray.
  • Calmodulin binding to pro-IL-1β is calcium-dependent and specific for the pro-form.
  • Both calcium and calmodulin are essential for nigericin-induced IL-1β secretion in THP-1 cells and primary human monocytes.

Conclusions:

  • Pro-IL-1β interacts with calmodulin after calcium influx.
  • This interaction is vital for the processing and release of IL-1β, shedding light on inflammation pathways.