By Sumit Chakraborty, Sushil Kumar Sharma, Asim Kumar Pal
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In addition, soluble Eph can also mediate signaling but are active only when they form clusters in the plasma membrane of the target cell. 1 Tyrosine Kinase Receptors Thus, Eph activate Eph-receptors only when membranebound, while soluble Eph are active when it aggregates into clusters. Tyrosine kinase receptors are single transmembrane ligand binding proteins that are able to phosphorylate their • Insulin and IGF-I bind to receptors that are already organized as tetramers inducing rearrangement of the transown tyrosine residues (autophosphorylation) located in the membrane chains by which both kinase domains come cytosolic region of the molecule.
1 (A) Organization of the seven transmembrane receptor and hormonal activation of the PKA pathway. The structure on the left represents an inactive receptor bound to the G-proteins. The structure on the right represents the reactions upon ligand binding to the receptor, including dissociation of the β/γ subunits from the G-protein complex, synthesis of cAMP, and activation of PKA. Activated PKA phosphorylates a variety of intracellular proteins including the transcription factor CREB. (B) Synthesis and degradation of cAMP.
In addition, the PKC C-subunit phosphorylates nuclear proteins, including the transcription factor CREB involved in transcriptional regulation of several genes (Chapter 5). The cAMP metabolizing enzymes, termed nucleotide phosphodiesterases (PDEs), hydrolyze cAMP into the inactive metabolite 5 -adenosine monophosphate (5 AMP) and regulate the overall activity of the PKA pathway (Fig. 1B). The PDEs belong to a large family of mammalian proteins, constituted of at least 20 different members that contain a central catalytic domain and an N-terminal regulatory domain that binds Ca2+ -CaM and the second messenger cGMP.