DEP domain-containing protein 1B (DEPDC1B)

DEP domain-containing protein 1B (DEPDC1B) is a cytoplasmic signaling protein characterized by an N-terminal DEP (Dishevelled, EGL-10, Pleckstrin) domain and a C-terminal RhoGAP-like (GTPase-activating protein) domain, although the latter lacks critical residues for intrinsic GAP activity[1][2]. DEPDC1B plays a central role in regulating the cell cycle: it promotes the dismantling of focal adhesions, facilitating cell detachment and proper mitotic entry, primarily by antagonizing RhoA-based signaling at adhesion sites[1][3]. It is most highly expressed during the G2/M phase and is overexpressed in various human cancers, where high levels of DEPDC1B correlate with increased tumor proliferation, migration, invasion, and poorer patient prognosis[1][3]. In normal skeletal myogenic cells, DEPDC1B drives proliferation and prevents premature differentiation; its knockdown leads to reduced proliferation and accelerated differentiation[1]. DEPDC1B does not directly act as an enzyme or receptor and currently has no known direct drug interactions[2]. Experimentally, DEPDC1B is considered an oncogenic driver and potential cancer biomarker, although no approved drugs target DEPDC1B directly.

Other names

XTP1XTP8HBV XAg-transactivated protein 8BRCC3 (historical)HBV XAg-transactivated gene 8 proteinHBxAg transactivated protein 1breast cancer cell 3

Potential mechanisms for drugs (if developed in the future) would likely involve modulation of cell proliferation, cell cycle progression, or RHOA signaling.