By Bertram Katzung, Susan Masters, Anthony Trevor
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Extra resources for Basic and Clinical Pharmacology, 11th Edition (LANGE Basic Science)
The receptor’s amino (N) terminal is extracellular (above the plane of the membrane), and its carboxyl (C) terminal intracellular. The terminals are connected by a polypeptide chain that traverses the plane of the membrane seven times. The hydrophobic transmembrane segments (light color) are designated by Roman numerals (I– VII). The agonist (Ag) approaches the receptor from the extracellular fluid and binds to a site surrounded by the transmembrane regions of the receptor protein. G proteins interact with cytoplasmic regions of the receptor, especially with portions of the third cytoplasmic loop between transmembrane regions V and VI.
Binding of hormone to the ligand-binding domain triggers release of hsp90. This allows the DNA-binding and transcrip- 4 5 Drug Outside cell R Membrane R E G Inside cell A B Y Y~P C D R FIGURE 2–5 Known transmembrane signaling mechanisms: 1: A lipid-soluble chemical signal crosses the plasma membrane and acts on an intracellular receptor (which may be an enzyme or a regulator of gene transcription); 2: the signal binds to the extracellular domain of a transmembrane protein, thereby activating an enzymatic activity of its cytoplasmic domain; 3: the signal binds to the extracellular domain of a transmembrane receptor bound to a separate protein tyrosine kinase, which it activates; 4: the signal binds to and directly regulates the opening of an ion channel; 5: the signal binds to a cell-surface receptor linked to an effector enzyme by a G protein.
Instead, a separate protein tyrosine kinase, from the Janus-kinase (JAK) family, binds noncovalently to the receptor. As in the case of the EGF receptor, cytokine receptors dimerize after they bind the activating ligand, allowing the bound JAKs to become activated and to phosphorylate tyrosine residues on the receptor. Phosphorylated tyrosine residues on the receptor’s cytoplasmic surface then set in motion a complex signaling dance by binding another set of proteins, called STATs (signal transducers and activators of transcription).
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