Cell Signaling and Phosphorylation in General Biology
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Activated phospholipase C cleaves the membrane phospholipid PIP₂ to produce IP₃ and diacylglycerol.
IP₃ (inositol triphosphate) and diacylglycerol.
IP₃ travels through the cytosol and binds IP₃-gated calcium channels in the ER membrane, releasing Ca²⁺ into the cytosol.
Calcium is released from the lumen of the endoplasmic reticulum (ER) into the cytosol.
Diacylglycerol remains in the membrane and helps activate conventional protein kinase C along with calcium.
Calcium, together with diacylglycerol, helps activate conventional protein kinase C.
Calcium binding to calmodulin regulates other target proteins in the cell.
Protein kinases transfer phosphate groups, usually from ATP, to target proteins, which can activate or inhibit them.
Protein phosphatases remove phosphate groups and help reset signaling components.
Loss of phosphatase activity can prolong phosphorylation-dependent signaling, affecting the pathway's duration.
Ligand removal, receptor inactivation, GTP hydrolysis, cAMP degradation, and restoration of low cytosolic calcium.
Phosphorylation can either activate or inhibit a protein depending on the target.
ATP usually donates the phosphate group transferred by protein kinases.
IP₃ binding to IP₃-gated calcium channels in the ER membrane triggers calcium release.
It helps terminate calcium-dependent signaling by returning calcium levels to baseline.