proteasome . . . polyubiquination

proteasome . . . glycosylation

lysosome . . . polyubiquination

lysosome . . . glycosylation

Ubiquitination

Glycosylation

Glycation

Hydroxylation

E1 activates ubiquitin molecules, E2 carries activated ubiquitin molecules to E3, and E3 covalently attaches activated ubiquitin molecules to a protein to mark it for degradation by a protease complex.

E1 transfers ATP to target proteins, E2 processes target proteins, and E3 degrades proteins through ATP-dependent complexes.

E1 senses cellular stress and activates E2, which phosphorylates E3 to conjugate ubiquitin to proteins to target them for post-translational modifications like acetylation.

E1 activates autophagosomes which fuse with proteins marked for degradation. E2 adds ubiquitin molecules to proteins within the autophagosome, and E3 activates acids to degrade the marked proteins.

E1, E2, and E3 are all redundant in their activity within the protein destruction pathway; each covalently attach ubiquitin to target proteins to mark them for degradation by the proteasome.

Proteasome

Lysosome

Peroxisome

Hydrolysis

None of these

Recognition of ubiquitin by the proteasome

Recognition of ubiquitin by the lysosome

Promotes exocytosis of the protein

None of the other answers

Promotes reprocessing through the Golgi apparatus

Proteolysis occurs in the lysosome but ubiquitin-mediated protein degradation is in the proteasome

These two processes are synonymous

Proteolysis is the degradation of organelles whereas proteins are degraded through ubiquitin-dependent mechanisms

Proteolysis occurs in only in the nucleus, but ubiquitin-mediated protein degradation occurs only in the cytoplasm

All of these are means of controlling protein concentration

Polyubiquination

Gene silencing

RNAi

Proteasome

Golgi

Vesicle

Endoplasmic reticulum

Lysosome