Charged multivesicular body protein 4C (CHMP4C)

Charged multivesicular body protein 4C (CHMP4C) is a protein-coding gene and a core component of the ESCRT-III complex, which orchestrates endosomal sorting, multivesicular body formation, and cytokinesis[1]. CHMP4C modulates the final membrane separation (abscission) during cell division by integrating regulatory signals from kinases such as Aurora B, affecting the timing and safety of chromosome distribution between daughter cells[3]. It is also involved in the biogenesis of extracellular vesicles and the release of enveloped viruses like HIV[1][2]. CHMP4C is up-regulated in multiple cancers and serves as a biomarker for poor prognosis and diagnosis in prostate and other malignancies, partially through its roles in cell cycle regulation and immune response modulation[2]. Targeting CHMP4C may sensitize tumors to standard chemotherapies (such as paclitaxel and 5-fluorouracil), but may also risk toxicity due to effects on normal cell division[2][3][1].

Other names

CHMP4CVPS32CShax3Vacuolar protein sorting-associated protein 32-3Snf7 homologue associated with Alix 3SNF7 homolog associated with Alix 3Chromatin-modifying protein 4cChromatin modifying protein 4ChSnf7-3hVps32-3SNF7-3

CHMP4C inhibition (siRNA or knockdown) reduces cancer cell proliferation, migration, and invasion through cell cycle inhibition. Higher CHMP4C expression also correlates with increased sensitivity to certain chemotherapies like Paclitaxel and 5-Fluorouracil.