The ubiquitin-dependent protein degradation pathway is essential for proteolysis of intracellular proteins and peptides. Enzymes that remove ubiquitin from ubiquitin-conjugated peptides, like USP28, affect the fate and degradation of intracellular proteins and are essential for maintenance of cell-free ubiquitin pools (1). USP28 is a deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. It plays a role in DNA damage induced by apoptosis by specifically deubiquitinating proteins of the DNA damage pathway, such as CLSPN. USP28 is also involved in G2 DNA damage checkpoint by deubiquitinating CLSPN, thus preventing its degradation by the anaphase promoting complex/cyclosome (APC/C) (2).
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