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Multiple Choice
Which protein modification is most closely linked to targeting proteins for degradation in eukaryotic cells?
A
Acetylation
B
Phosphorylation
C
Glycosylation
D
Ubiquitination
Verified step by step guidance
1
Understand the concept of protein modifications: Protein modifications are chemical changes made to proteins after their synthesis. These modifications can alter protein function, localization, or stability.
Learn about ubiquitination: Ubiquitination is a post-translational modification where ubiquitin, a small regulatory protein, is covalently attached to a target protein. This process often marks proteins for degradation via the proteasome in eukaryotic cells.
Compare ubiquitination with other modifications: Acetylation typically regulates gene expression by modifying histones, phosphorylation is involved in signal transduction and enzyme activity regulation, and glycosylation affects protein folding and stability. None of these are primarily linked to protein degradation.
Recognize the role of ubiquitination in protein degradation: Ubiquitination tags proteins for destruction by the proteasome, a large protein complex responsible for degrading and recycling damaged or unneeded proteins in eukaryotic cells.
Conclude that ubiquitination is the correct answer: Based on its function in targeting proteins for degradation, ubiquitination is the protein modification most closely linked to this process in eukaryotic cells.