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Cell Communication
Cell Communication
The images and text in this file are from Campbell, Reece, and Mitchell: Biology (5th edition, I think)
2. Binding of the factors to receptors induces changes in the cells that lead to their fusion, or mating.
3. The resulting "a"/alpha. cell combines in its nucleus all the genes from the "a" and alpha cells.
(a) Animals have two main kinds of local chemical signaling. In paracrine signaling, a secreting cell acts on nearby target cells by discharging molecules of a local regulator into the extracellular fluid. In synaptic signaling, a nerve cell releases neurotransmitter molecules into a synapse, the narrow space between the transmitting cell and the target cell, here another nerve cell. (b) Hormones signal target cells at much greater distances. In animals, specialized endocrine cells secrete hormones into body fluids, often the blood. Hormones may reach virtually all body cells, but, as with local regulators, only specific target cells recognize and respond to a given chemical signal. (Plants also use hormones for signaling from one part of the plant to another.)
(b) Two cells in an animal may communicate by interaction between molecules protruding from their surfaces.
From the perspective of the cell receiving the message, cell signaling can be divided into three stages: signal reception, signal transduction, and cellular response. When reception occurs at the plasma membrane, as shown here, the transduction stage is usually a pathway of several steps, with each molecule in the pathway bringing about a change in the next. The last molecule in the pathway triggers the cell's response.
(b) When the signal molecule binds to the receptor, the receptor changes shape in such a way that it binds and activates the G protein. A molecule of GTP replaces the GDP on the G protein. The active G protein (moving freely along the membrane) binds to and activates the enzyme, which triggers the next step in the pathway leading to the cell's responses.
(c) The G protein then catalyzes the hydrolysis of its GTP and dissociates from the enzyme, becoming available for reuse. All three proteins remain attached to the plasma membrane.
A large family of eukaryotic receptor proteins have this secondary structure: The single polypeptide, represented as a ribbon, has seven transmembrane alpha helices. Specific loops correspond to the sites where signal molecules and G-protein molecules bind. The alpha helices are depicted as cylinders for emphasis.
(b) When signal molecules (such as a growth factor) attach to their binding sites, two polypeptides aggregate, forming a dimer. Using phosphate groups from ATP, the tyrosine-kinase region of each polypeptide phosphorylates the tyrosines on the other polypeptide. In other words, the dimer is both an enzyme and its own substrate. Now fully activated, the receptor protein can bind specific intracellular proteins, which attach to particular phosphorylated tyrosines and are themselves activated. Each can then initiate a signaltransduction pathway leading to a specific cellular response. Tyrosine-kinase receptors often activate several different signal-transduction pathways at once, helping regulate such complicated functions as cell reproduction (cell division). Inappropriate activation of these receptors can lead to uncontrolled cell growth--cancer.
A phosphorylation cascade
This hypothetical signaling pathway begins when a signal molecule binds to a membrane receptor. The receptor then activates a relay molecule, which activates protein kinase 1. Active protein kinase 1 transfers a phosphate from ATP to an inactive molecule of protein kinase 2, thus activating this second kinase. In turn, active protein kinase 2 catalyzes the phosphorylation (and activation) of protein kinase 3. Finally, active protein kinase 3 phosphorylates a protein that brings about the cell's final response to the signal. The dashed arrows represent inactivation of the phosphorylated proteins, making them available for reuse; enzymes called phosphatases catalyze the removal of the phosphate groups. The active and inactive proteins are represented by different shapes to remind you that activation is usually associated with a change in molecular conformation.
Cyclic AMP
Cyclic AMP (cAMP) is made from ATP by adenylyl cyclase, an enzyme embedded in the plasma membrane. The enzyme is activated as a consequence of binding of a signal molecule (such as the hormone epinephrine) to a membrane receptor. Cyclic AMP functions as a second messenger that relays the signal from the membrane to the metabolic machinery of the cytoplasm. Cyclic AMP is inactivated by phosphodiesterase, an enzyme that converts it to inactive AMP.
Calcium ions (Ca21) and inositol trisphosphate (IP3) function as second messengers in many signal-transduction pathways. The process is initiated by the binding of a signal molecule to either a G-protein-linked receptor (left) or a tyrosine-kinase receptor (right). The circled numbers trace the former pathway. 1. A signal molecule binds to a receptor, leading to 2. activation of an enzyme called phospholipase C. 3. This enzyme cleaves a plasma-membrane phospholipid called PIP2 into DAG and IP3 (inset). Both can function as second messengers. 4. IP3, a small molecule, quickly diffuses through the cytosol and binds to a ligand-gated calcium channel in the ER membrane, causing it to open. 5. Calcium ions flow out of the ER (down their gradient), raising the Ca21 level in the cytosol. 6. The calcium ions activate the next protein in one or more signaling pathways, often acting via calmodulin, a ubiquitous Ca21-binding protein. DAG functions as a second messenger in still other pathways.