Final answer:
Eukaryotic cells manage misfolded proteins primarily through autophagy and ubiquitination, where ubiquitin tags the proteins for degradation by the proteasome and autophagy uses vesicles to degrade them via lysosomes.
Step-by-step explanation:
Eukaryotic cells use several mechanisms to manage misfolded proteins. Two key processes involved in this task are autophagy and ubiquitination. In ubiquitination, a small protein called ubiquitin targets the misfolded proteins for degradation. This tagged protein is conveyed to the proteasome, which is a large complex that dismantles the protein. Autophagy, on the other hand, involves the formation of a double-membraned vesicle called an autophagosome that envelops the misfolded protein and fuses with a lysosome for degradation. While phagocytosis and exocytosis are important membrane transport mechanisms, phagocytosis involves the engulfment of large particles, and exocytosis is related to the secretion of substances out of the cell. Therefore, the correct mechanisms that eukaryotic cells use for dealing with some misfolded proteins are A. Autophagy and B. Ubiquitination.