Signals, Communication, and Junctions - GRE

Gap junctions can be thought of as small tunnels between cells. They allow for the immediate transport of ions and molecules between the cells. Gap junctions are prominent in cardiac myocytes, and help spread action potentials via electrical synapses to coordinate the contraction of the heart.

The movement of substances between cells is most commonly controlled by tight junctions. These junctions can be regulated, which can alter how strongly they resist the movement of material between cells, like those in the digestive tract during absorption.

Most of the other proteins listed are structural, but do not form any kind of pore or channel through which an electrical message can cross. Connexins are required for this function of gap junctions.

While each of the proteins listed contribute to cell structure and function, the tight junction requires claudins and occludins to anchor the cytoskeleton of two adjacent cells to one another. These are the primary structural components of tight junctions.

Adherens junctions are formed by linking the actin cytoskeleton to transmembrane proteins known as cadherins. Cadherins are capable of interacting with other cadherins from neighboring cells on the exoplasmic face of the cell membrane. This interaction forms a physical link essentially connecting the actin cytoskeletons of the two adjacent cells, thus promoting force transduction.

Desmosomes are another type of cell junction that link the intermediate filaments of the cytoskeleton to cadherins.

Of the choices, only adherens junctions and hemidesmosomes are responsible for anchoring the extracellular matrix. This is accomplished by associating the actin cytoskeleton (for adherens junctions) or the intermediate filament cytoskeleton (for hemidesmosomes) with transmembrane proteins known as integrins. Integrins interact with the extracellular matrix.

Desmosomes are responsible for anchoring adjacent cells to one another by connecting their intermediate filament cytoskeletons with cadherins. Gap junctions connect the cytoplasm of adjacent cells and allow the free flow of small molecules between them.

"Gap junctions prevent molecules and ions from traveling between cells in the extracellular space" is incorrect because this describes the function of tight junctions. Gap junctions electrically couple two cells by permitting the formation of small channels that connect two cells.

The peak of an action potential signals the inactivation of sodium channels. This effectively prevents more sodium from entering the cell and halts the depolarization that was previously occurring, resulting in a maximum depolarization value. Potassium channels remain open, and are the cause for the membrane potential to start dropping (positive charge is leaving the cell). The sodium-potassium pump does not stop during this process. In fact, its continued function is essential for eventually restoring the resting membrane potential.

Neurotransmitters will bind their respective receptors on the post-synaptic membrane, which is a muscle in this case. This binding causes changes to other proteins on that membrane, which results in an opening of ion channels. The muscle then depolarizes due to the influx of positively charged ions, and this can be measured as a positive change in the muscle membrane potential.

Depolarization, also known as the rising phase, occurs when the membrane potential goes from being negative to positive very quickly. This is instigated by the influx of ions through the open voltage gated channels, and the positive ions make the cell more positive relative to the resting potential.

The sodium-potassium pump maintains the resting membrane potential by utilizing 1 ATP to transport 2 potassium ions into the cell, and pumping 3 sodium ions out, which makes the inside of the cell negative relative to the outside of the cell.

Before answering this question, consider what types of hormones would not attach to a membrane bound receptor. Steroid hormones can simply diffuse through the plasma membrane, so they do not need to attach to a receptor there. Cortisol, testosterone, and estrogen are all steroid hormones. This leaves insulin as the only acceptable answer. In fact, insulin attaches to a receptor tyrosine kinase on the outside of cells.

The correct answer is elicit innate immune responses by recognizing microbial associated molecular patterns. TLRs are pattern recognition transmembrane receptors that recognize bacterial components, such as lipopolysaccharides and flagellin, and viral components such as single stranded DNA. Upon recognition by the leucine rich region, TLRs dimerize to facilitate signal transduction (via the toll-interleukin region domain) to downstream pathways to promote inflammation and recruitment of macrophages.

The sodium-potassium pump is a type of active transport that brings sodium out of the cell and potassium into the cell. This is in the opposite direction of their natural gradient. The fact that it is going in the opposite direction requires this pump to need energy, or, ATP.

G protein coupled receptors are by far the largest class of cell surface receptors. They can respond to a large variety of extracellular signaling molecules, and can elicit a great deal of responses inside cells. With such diversity, it should come as no surprise that not all GPCRs will increase cAMP levels in the cell. In fact, many can display an inhibitory role, and decrease cAMP levels by preventing its production.

Second messengers are the molecules in a signal transduction pathway that will activate an intracellular response. Epinephrine is a hormone that will bind a receptor on the exoplasmic face of the cell, making is a first messenger. G subunits interact with adaptor proteins that will then stimulate the production of second messengers. Receptor tyrosine kinases are examples of receptor proteins that will bind first messengers. cAMP, however, is a widely used second messenger that is involved in the activation of many pathways and signal amplification in the cytosol.

A second messenger response is created in cells that use signal transduction, meaning that the signaling molecules attach to a receptor on the outside of the cell. Steroid hormones are largely nonpolar, and can enter the cell in order to affect cellular processes at the level of transcription. As a result, they do not need to rely on second messenger pathways in order to elicit a response.

When MAP Kinase signaling is activated, the receptors auto-phosphorylate to activate the signal transduction, which leads to the binding of GTP to Ras. Ras is activated when bound to GTP. Ras then activates downstream MAP Kinases, which lead to a phosphorylate cascade that eventually uses ATP to phosphorylate transcription factors. The phosphorylated transcription factors then go on to alter gene expression in the cell.

Therefore, the correct answer in this question is that transcription factors are phosphorylated using ATP molecules.

The correct answer is scaffold proteins. By bringing signaling transduction pathway proteins into complex, scaffolds rapid promote activation (often by phosphorylation) of the pathway proteins to effect a biological output. Kinases phosphorylate substrates, ligases bind substrates, and transcription factors regulate transcription, however, these proteins do not complex signaling pathway intermediates to amplify a signal. Adaptor proteins are involved in signal transduction, however, their role is mainly in cross-talk between different pathways upon a certain stimulus or activation of a given signaling pathway.

The correct answer is apoptosis. Apoptosis, commonly referred to as "programmed cell death", is an energy dependent mechanism that produces apoptotic bodies that are engulfed by the immune system. Mitochondrial leakage of cytochrome c can activate caspase pathways to proteolytically cleave host intracellular proteins. While necrosis is a mechanism for cell death, it is energy-independent and much less controlled and is characterized by organelle swelling and disintegration. Autophagy is a mechanism of cell death in which autophagosomes and autolysosomes are formed and degrade intracellular proteins. Paraptosis is a specific form of cell death that occurs by cell-surface receptors initiating cell death signals in the absence of normal ligands.