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Anaphase-promoting complex subunit 10 (ANAPC10/APC10), also known as Doc1, is a core component of the anaphase-promoting complex/cyclosome (APC/C), a large, multisubunit E3 ubiquitin ligase essential for cell cycle progression. ANAPC10 plays a critical role in substrate recognition and the processive ubiquitination of key cell cycle regulators such as cyclin B1 and securin, thereby ensuring proper mitotic progression by mediating their targeted degradation by the proteasome. Its interaction with other core APC/C subunits and coactivators (CDC20, CDH1) forms a bipartite receptor that determines substrate specificity and order of protein turnover, critical for transitioning from metaphase to anaphase and mitotic exit. Dysregulation of ANAPC10 expression has been implicated in cancer, where elevated levels may contribute to tumor proliferation, metabolic reprogramming, and autophagy. Additionally, ANAPC10 is expressed in germ cells and may play a role in meiotic progression. The APC10 domain is recognized as a versatile structural element important for substrate binding and specificity in ubiquitination pathways. Overall, ANAPC10 is indispensable for normal cell division and its aberrant function is linked to diseases of cell cycle control.
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