The correct answer is recognition of ubiquitin by the proteasome. Ubiquitin-mediated protein degradation by the proteasome is a well characterized method of specific protein degradation. The protein targeted for degradation is phosphorylated, then ubiquitinated. The proteasome recognizes these distinct ubiquitin chains and degrades the protein. Protein degradation can also occur through the lysosome, but this is independent of ubiquitination and is less specific. The golgi complex is involved in protein folding and modification of recently translated amino acid chains. 

The correct answer is that proteolysis occurs in the lysosome but ubiquitin-mediated protein degradation is in the proteasome. Proteolysis-lysosomal degradation is non-selective and is activated upon cellular starvation. ubiquitin-mediated protein degradation is highly specific and functions to promote a wide range of cellular processes. 

Older proteins in our bodies need to be degraded once they become damaged or no longer necessary. One way that the cell tags these proteins is by adding a ubiquitin tag, which can then be recognized by a proteasome, leading to the proteins' deconstruction.

Clathrin coats are often seen trafficking vesicles from the Golgi apparatus to the plasma membrane. Clathrin protein is used to facilitate membrane invagination and vesicle formation, as well as direct vesicle release.

COPI coats are seen in vesicles headed from the Golgi apparatus back to the endoplasmic reticulum. COPII coats are seen in vesicles headed towards the Golgi apparatus from the endoplasmic reticulum.

Actin and microtubules have similar chemical properties. They maintain a nucleotide gradient (ADP/ATP for actin and GDP/GTP for microtubules) across their structures and have two distinct polarized ends. Intermediate filaments do not have either of these characteristics. For that reason, motor proteins associate with actin and microtubules as opposed to intermediate filaments. The polarity of the microtubules and actin allow the motor proteins to become oriented, transporting cargo in a particular direction along the structure. These motor proteins (such as myosin, dynein, and kinesin) are essential for vesicular transport.

Both the actin microfilament cytoskeleton and the microtubule cytoskeleton serve important functions in vesicular transport. They serve as the structures upon which motor proteins move, essentially providing a directional tract for vesicular transport. Motor proteins, such as kinesin, associate with vesicles and bring them from one area of the cell to the other along the directional filaments.

The intermediate filament cytoskeleton lacks the polarity displayed by actin microfilaments and microtubules, making it not very useful for vesicular transport.

This requires knowing that SNARE proteins are required for proper vesicle fusion to the membrane, thereby permitting exocytosis of neurotransmitters into the synaptic cleft and activating the next target; muscle in this case. Paralysis comes because the muscle is not receiving any input once the toxin has cleaved/destroyed the SNARE proteins. 

Actin (microfilaments) is a cytoskeletal component, and myelin is an axon wrapping component; not molecular motors. Kinesin is a motor that moves in the plus-end direction, away from the MTOC. Dynein is the correct answer; it moves in the minus-end direction towards the MTOC.

Synaptotagmin is a calcium sensor that is associated with the vesicle to be exocytosed. In a high calcium environment, synaptotagmin becomes activated and interacts with syntaxin, a SNARE protein docked in the membrane from which the vesicle will be exocytosed. This interaction permits selective exocytosis during processes such as neurotransmission when there is a large calcium influx, indicating a message must be relayed to the next cell. 

Bax and Bak dimerize to form a pore in the mitochondria outer membrane, which allows cytochrome c to escape into the cytosol. When cytochrome c is found in the cytosol, procaspase becomes activated and is cleaved into caspase. Once the caspase cascade begins the cell is destined for death.

Bax and Bak have nothing to do with the apoptosome and, while Bcl2 does block Bax and Bak from dimerizing, Bax and Bak do not prevent the action of Bcl2.