Ubiquitin Structure & Function: Difference between revisions
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There are 3 different types of ubiquitin conjugates known: | There are 3 different types of ubiquitin conjugates known: | ||
=== Ubiquitinylation === | === Ubiquitinylation === | ||
Ubiquitinylation simply refers to the isopeptide bond formations between the carboxyl-terminal of ubiquitin and the ε-amino acid side chain of the target proteins. | |||
=== Multi-ubiquitinylation === | |||
This type of ubiquitin conjugate is a critical step in the process of protein degradation. This process refers to the addition of single ubiquitin molecules to numerous lysine residues on a target protein. | |||
=== Polyubiquitinylation === | |||
This conjugate formation is the most important process in protein degradation as it officially targets the protein for degradation. Polyubiquitinylation refers to the addition of several ubiquitin molecules to a single lysine residue on a protein. Isopeptide bonds are formed between the carboxyl-terminus of one ubiquitin and a lysine residue on an adjacent ubiquitin. | |||
=Diseases= | =Diseases= | ||
=References= | |||
<references/> | <references/> | ||
