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Related Concept Videos

IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

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 produces two-second...
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Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

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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Calmodulin-dependent Signaling01:16

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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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cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

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Related Experiment Video

Updated: May 10, 2026

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Published on: July 26, 2019

PPP3CC feedback regulates IP3-Ca2+ pathway through preventing ITPKC degradation.

Pu Li1, Peng Zhang, Ying Lin

  • 1State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, PR China.

Frontiers in Bioscience (Landmark Edition)
|June 11, 2013
PubMed
Summary

Researchers discovered PPP3CC interacts with ITPKC, a gene linked to Kawasaki disease. PPP3CC stabilizes ITPKC levels, impacting the IP3-Ca2+ signaling pathway crucial for immune responses.

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Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes

Published on: January 7, 2013

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Signaling

Background:

  • Inositol trisphosphate kinase C (ITPKC) is a susceptibility gene for Kawasaki disease.
  • ITPKC regulates intracellular calcium (Ca2+) levels and calcineurin/NFAT signaling.
  • Understanding ITPKC regulation is crucial for Kawasaki disease research.

Purpose of the Study:

  • To identify novel proteins interacting with ITPKC.
  • To elucidate the functional role of ITPKC-interacting proteins in cellular signaling.
  • To investigate the impact of these interactions on the IP3-Ca2+ pathway.

Main Methods:

  • Yeast two-hybrid screening to identify interacting proteins.
  • GST pull-down and co-immunoprecipitation assays for interaction validation.
  • Fluorescent microscopy for protein co-localization studies.
  • Western blotting to assess protein levels and phosphorylation status.

Main Results:

  • A novel ITPKC-interacting protein, PPP3CC, was identified and validated.
  • PPP3CC and ITPKC co-localize in the cell cytoplasm.
  • PPP3CC enhances ITPKC protein stability by inhibiting its phosphorylation and subsequent degradation.
  • PPP3CC levels negatively correlate with cellular inositol trisphosphate (IP3) levels.

Conclusions:

  • PPP3CC is a novel regulator of ITPKC stability and function.
  • PPP3CC plays a significant role in modulating the IP3-Ca2+ signaling pathway.
  • These findings provide new insights into the molecular mechanisms underlying Kawasaki disease pathogenesis.