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FBXO8, or F-box protein 8, is a human protein encoded by the FBXO8 gene and is part of the F-box family, characterized by the F-box domain involved in protein ubiquitination[3]. FBXO8 serves as a substrate recognition subunit in the SCF (SKP1-Cullin-F-box) E3 ubiquitin ligase complex, regulating proteasomal degradation of key proteins[2][3]. It mediates noncanonical ubiquitination of the small GTPase Arf6, suppressing invasive activity in breast cancer cells and contributing to membrane remodeling and cell migration[1]. Loss or dysfunction of FBXO8 has been associated with increased cancer cell invasiveness, supporting its role as a tumor suppressor and potential target for cancer therapy[1][2][3]. The molecular actions and expression of FBXO8 are subject to modulation by epigenetic and post-translational mechanisms, making it a central player in cell signaling, protein turnover, and potentially tumor immune regulation[2][3].
For theoretical drugs: inhibition or restoration of FBXO8 function would modulate Arf6 activity and substrate ubiquitination, affecting cell invasion and tumor suppressive mechanisms
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