Cellular Communications and Junctions - AP Biology

Antagonists are ligands that inhibit receptors; thus, they create a receptor blockade. Some antagonists are able to bind irreversibly to the receptor by covalent bonds, blocking the receptor.

G protein-coupled receptors are part of a large class of receptors involved in intercellular signaling. Structurally, G protein-coupled receptors have an extracellular N terminus, seven transmembrane helices, three intracellular loops, three extracellular loops, and an intracellular C terminus. The ligand-binding domain is within the transmembrane helices.

When a protein is active in it’s native state, it is said to be constitutively active. In the case of protein receptors, a receptor is constitutively active when it is active without binding to a ligand.

Endocrine signals are signals from distance cells that move using the bloodstream, paracrine signals are signals used to communicate between cells in close proximity, and autocrine signals are signals that are received by the same cell in which the signal originated. Paracrine signals are signal are short-lasting, whereas endocrine signals are long-lasting.

Endocrine signals are signals from distance cells that move using the bloodstream, paracrine signals are signals used to communicate between cells in close proximity, autocrine signals are signals that are received by the same cell in which the signal originated, and direct signaling occurs across gap junctions through the movement of small molecules (such as Calcium ions).

G-protein linked receptors are a type of cell-surface receptor that, when unbound by a ligand, consists of an alphaGDP subunit and a beta gamma subunit. When a ligand binds, GDP is exchanged for GTP, which causes the alphaGTP subunit to dissociate from the receptor and the beta gamma subunit. Then, the alphaGTP and beta gamma subunits can activate other molecules in the cell.

Endocrine signals are signals from cells that move using the bloodstream and signal to distant cells, paracrine signals are signals used to communicate between cells in close proximity, autocrine signals are signals that are received by the same cell in which the signal originated, and direct signaling occurs across gap junctions through the movement of small molecules (such as Calcium ions).

Endocrine signals are signals from cells that move using the bloodstream to signal to distant cells, paracrine signals are signals used to communicate between cells in close proximity, autocrine signals are signals that are received by the same cell in which the signal originated, and direct signaling occurs across gap junctions through the movement of small molecules (such as Calcium ions). Beta cell in the pancreas produce insulin, a hormone, which is secreted into the bloodstream.

The membrane of the cell is a phospholipid bilayer, which allows hydrophobic molecules to diffuse through it. Small, hydrophobic ligands are able to diffuse through the plasma membrane. Nitric oxide is lipophilic, readily dissolving in lipids, and can diffuse across the plasma membrane. Steroid hormones are hydrophobic, and can thus diffuse across the plasma membrane. Water-soluble ligands cannot diffuse across the plasma membrane to enter a cell.

Calcium is a widely used second messenger of signal transduction. Calcium ions can function as a second messenger because its concentration within cell cytosol is much lower than outside the cell, and it is actively transported out of the cell by protein pumps. Modulation in calcium levels is used to transmit signals from both G protein and receptor tyrosine kinase signaling cascades and is involved in such functions as muscle contractions and synaptic signaling.

The other common second messenger molecule is cAMP.

After a ligand binds to receptor tyrosine kinases, the receptors need to form a dimer to foster activation of their tyrosine kinase activity. After dimerization, a phosphate is transferred from ATP to the amino acid tyrosine at specific sites on the cytoplasmic region of receptor. The phosphorylation of the tyrosines provides a site where other cellular proteins can bind and further relay the signal from the receptor to the cell.

Intracellular receptors are found in the cytoplasm of the cell. Ligands for intracellular receptors are usually small molecules that can pass through the cell membrane, and include substances such as steroid hormones. Upon binding and activation, intracellular receptors bind specific DNA motifs in the nucleus and function as transcription factors, directly changing expression of genes.

In contrast, transmembrane receptors are embedded in the plasma membrane and bind extracellular ligands to mediate intracellular responses. Ligand binding to transmembrane receptors often initiates a signal cascade or mediates channel activity within the membrane of the cell.

Seeing as peptide hormones are generally large, water-soluble molecules, they cannot transverse the phospholipid membrane. Instead, they must act through a membrane-bound protein receptor. Steroid hormones are generally small, fat-soluble organic molecules that can easily travel through the phospholipid membrane and the nuclear membrane. They can then act on transcription factors or interact directly with DNA. Both peptide and steroid hormones initiate changes within the cell; they simply do so by different mechanisms.

Cell signaling is the process used by cells to communicate and control cellular activities. It can occur both within and between cells. The correct sequence of events that takes place during cell signaling is as follows: reception, transduction, and response. The reception stage is the detection of a signal, typically by a receptor on the cell surface. Next, transduction is characterized by the transmission of signals from the cell’s exterior to its interior by way of proteins. Finally, the response is the subsequent cellular reaction to the signaling. Cell signaling is critically important in normal cell function and widely diversified.

G protein-coupled receptors are only found in eukaryotes including yeast cells and animal cells. Bacteria cells are prokaryotes, and therefore do not contain G protein-coupled receptors. Even though yeast cells are single-celled, they possess all the characteristics of eukaryotic cells.

G proteins are a class of protein signaling molecules that are activated by G protein-coupled receptors (GPCRs). When a ligand binds to the transmembrane domain of GPCRs, the GPCR undergoes a conformational change. This conformational change activates the G protein, which binds to GTP rather than lower energy GDP. The active G protein can then dissociate and transmit the signal by interacting with other proteins.

Tyrosine kinase receptors exist as single monomers but possess the capability to polymerize. Tyrosine kinase receptors have a transmembrane domain, an extracellular N terminus, and an intracellular C terminus. When a ligand binds to the extracellular N terminus, the tyrosine kinase receptor dimerizes. There are multiple models of receptor dimerization. One of the models is that dimerization is aided by the ligand itself, which binds to the N termini of both tyrosine kinase receptors. Another is that dimerization occurs after each tyrosine kinase receptor monomer binds to a ligand. A final model postulates that the binding of a ligand induces a conformation change that allows dimerization.

Tyrosine kinase receptors are composed of a transmembrane domain, an extracellular N terminus, and an intracellular C terminus. Ligand binding to the extracellular N terminus stimulates receptor dimerization. The dimerization stimulates kinase activity on the intracellular C terminus, leading to the autophosphorylation of the tyrosine residues on the C terminus. This phosphorylation of tyrosine residues creates binding sites for relay proteins, which are then phosphorylation by the tyrosine kinase receptors. The phosphorylated relay proteins then transmit the signal to other cellular pathways.

Tyrosine kinase receptors are fully activated when they bind to an extracellular ligand, dimerize, and then autophosphorylate at tyrosine residues on the C terminus. The signal is not transduced until relay proteins are phosphorylated by the tyrosine kinases. These relay proteins can then stimulate a phosphorylation cascade that initiates signaling pathways, which regulate nuclear gene transcription

When inactive, ion gated receptors are closed. When a ligand binds, the channel undergoes a conformational change and opens: creating a tunnel. This conformational change does not last for a long period of time; the ligand soon dissociates and the ion channel closes.