YY1 and neoplasm: In contrast, Th2‐CD4+ T cells may subvert Th1 responses, providing a microenvironment conducive to tumor progression.[52, 53] Additionally, MAGEA6 has been implicated in modulating protein ubiquitination by enhancing the activity of E3 ubiquitin ligases, leading to the ubiquitination and degradation of AMPK.[31] Our study builds on this by demonstrating that MAGEA6 interacts with the deubiquitinase USP10, inhibiting the ubiquitination and degradation of YY1 protein, further emphasizing its significant role in ubiquitination regulation.