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 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. 

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.

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.

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.  

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.

Nuclear import and export do not require post-translational modifications. The nuclear localization sequence or the nuclear export sequence is contained within the amino acid sequence itself (primary structure), and does not require and special modification.

For targeting to the proteasome, proteins must be ubiquinated. To target a protein to the lysosome the addition of a mannose-6-phosphate is commonly made. 

When considering a protein creating/secreting cell, the organelles that are responsible for packaging and secreting the proteins will be most important. Starting at the beginning, proteins will be translated using the ribosomes found on the rough endoplasmic reticulum. Those will then be sent to the golgi apparatus for proper packaging. Those packages will then be released from the cell. The smooth endoplasmic reticulum will not be a vital organelle for protein creation and secretion.