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Protein kinase A and two phosphatases are components of the inositol 1,4,5-trisphosphate receptor macromolecular signaling complex
- Source :
- The Journal of biological chemistry. 277(42)
- Publication Year :
- 2002
-
Abstract
- The inositol 1,4,5-trisphosphate receptor (IP3R) is a ubiquitously expressed intracellular calcium (Ca(2+)) release channel on the endoplasmic reticulum. IP3Rs play key roles in controlling Ca(2+) signals that activate numerous cellular functions including T cell activation, neurotransmitter release, oocyte fertilization and apoptosis. There are three forms of IP3R, all of which are ligand-gated channels activated by the second messenger inositol 1,4,5-trisphosphate. Channel function is modulated via cross-talk with other signaling pathways including those mediated by kinases and phosphatases. In particular IP3Rs are known to be regulated by cAMP-dependent protein kinase (PKA) phosphorylation. In the present study we show that PKA and the protein phosphatases PP1 and PP2A are components of the IP3R1 macromolecular signaling complex. PKA phosphorylation of IP3R1 increases channel activity in planar lipid bilayers. These studies indicate that regulation of IP3R1 function via PKA phosphorylation involves components of a macromolecular signaling complex.
- Subjects :
- Time Factors
Immunoblotting
Lipid Bilayers
Receptors, Cytoplasmic and Nuclear
Biology
Endoplasmic Reticulum
Ligands
Biochemistry
chemistry.chemical_compound
Cerebellum
Cyclic AMP
Phosphoprotein Phosphatases
Animals
Inositol 1,4,5-Trisphosphate Receptors
Protein phosphorylation
Inositol
Phosphorylation
Protein kinase A
Molecular Biology
Kinase
Calcium-Binding Proteins
Microfilament Proteins
Brain
Cell Biology
Inositol trisphosphate receptor
Cyclic AMP-Dependent Protein Kinases
Precipitin Tests
Phosphoric Monoester Hydrolases
Cell biology
Rats
DNA-Binding Proteins
Electrophysiology
chemistry
Second messenger system
Oocytes
Calcium
Calcium Channels
Signal transduction
Protein Binding
Signal Transduction
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 277
- Issue :
- 42
- Database :
- OpenAIRE
- Journal :
- The Journal of biological chemistry
- Accession number :
- edsair.doi.dedup.....54abe8b1f877dddbdb397db5d89d889c