The excitatory postsynaptic potentials produced from a presynaptic neuron leads to the generation of the action potentials. The presynaptic neuron unloads the neurotransmitters in response to the excitatory postsynaptic potentials. The post-synaptic neurons have the receptors for the linkage of the neurotransmitters released into the synaptic cleft. The joining of the neurotransmitters causes the opening of numerous ion channels. The opening of such ion channels alters the permeability of the membrane and concurrently alters the membrane potentials. The synapse is excitatory as the union of the neurotransmitter elevates the voltage. The hyperpolarization of the membrane due to the coupling of the neurotransmitter is inhibitory.
Intracellular signaling: The elongation of the tip of the axon is promoted by the function of phosphoinositide 3-kinase(PI3K) and the lack of activity of PI3K can disrupt the development of the axon. The PI3k in turn stimulates the production of phosphatidylinositol triphosphate for provoking the elongation of the axon.
Extracellular signaling: Numerous extracellular signals are conveyed through the extracellular matrix to stimulate the development of the axon in a neuron. The extracellular signaling factors connected with the axonal development include extracellular matrix, neurotrophic factors, proteins, adhesion molecules. The elongation of the axon is activated by the enzyme called plasma membrane ganglioside sialidase.
Different Extracellular Messenger Systems Involved in Signal Transduction
Ligand-gated ion channels: The ligand-gated ions channel consists of a receptor protein and ligand, which on connecting with the receptor protein will induce a conformational change in the protein. This will open the ion channel for the propagation of ions. This type of signaling system is observed in the neural synapse. The ions transported into the cell will stimulate the production of an action potential. These action potentials will result in the depolarization of the membranes located in the post-synaptic cells. This will in turn opens the voltage-gated ions channels of the cell. The calcium ions are conveyed into the cell through the ligand-gated ion channels and these ions will function as the second messengers for the stimulation of signal transduction cascades.
Toll-like receptors: The adapter molecules residing within the cytoplasm are employed by the toll-like receptors for the propagation of a signal. These molecules include translocating chain-associating membrane protein (TRAM), TIR-domain-containing adapter-inducing IFN-β(TRIF), MyD88-adapter-like protein (TIRAP), and myeloid differentiation primary response protein 88 (Myd88). These adaptor molecules in turn stimulate intracellular substances such as the TBK1, IRAK1, Ikki, and IRAK4. The stimulation further mediates the suppression or induction of genes. Numerous genes are activated by the signaling performed by the Toll-like receptors and thus it is an important method for the modulation of the gene.
Integrins: The integrins are generated by numerous cells and have a significant role in the cellular attachments. The transduction of the signals originated from the extracellular matrix is carried out by the integrins. The chief extracellular components influenced by the integrins include collagen and fibronectin. The conformation la change of the protein takes place with the binding of the ligand to the domains in the external surface of the cell. The clustering of integrins takes place at the plasma membrane for stimulating signal transduction. The coordinator proteins such as the integrin-linked kinases are employed for the signal transduction performed by the integrins. This toll-like receptor manages various functions including differentiation, proliferation, and apoptosis.
Tyrosine -specific protein kinases: The extracellular domains of the tyrosine kinase protein adjoin with the ligand and the intracellular domain consists of kinase activity. The dimerization of the receptor tyrosine kinases takes place before the signal transduction. The stabilization of the dimer takes place with the connection between the receptor and the ligands. The autophosphorylation of the tyrosine residues takes place with the interaction taking place between the domains residing in the cytoplasm.
G-Protein Coupled Receptors
These receptors encompass a set of integral transmembrane proteins composed of seven transmembrane areas connected to a heterotrimeric G protein. The important groups of G-protein coupled receptors include secretin like, rhodopsin-like, adhesion, metabotropic glutamate, and smoothened. The coupling of the inactive G protein and the receptor will stimulate the signal transduction process in the G protein-coupled receptor. The active form of the G protein is formed from the binding of the ligand and the receptor.
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