Charged multivesicular body protein 4B (CHMP4B)

Charged multivesicular body protein 4B (CHMP4B) is a core component of the ESCRT-III complex, which plays a critical role in sorting endocytosed surface receptors into multivesicular endosomes for degradation, as well as in the scission of membrane necks during cytokinesis and the budding of enveloped viruses such as HIV-1. CHMP4B assembles into membrane-attached spiral or filamentous scaffolds that drive or stabilize membrane deformation and budding processes. Interaction with proteins such as ALIX (PDCD6IP) is essential for its function in the ESCRT pathway. Mutations in CHMP4B disrupt vesicular trafficking and are associated with autosomal dominant cataracts. Although this protein is biologically important, it is not currently the target of clinically approved drugs, but it has relevance in research on cell division, viral replication, and hereditary disease.

Other names

SNF7-2VPS32BVps32-2SHAX1C20orf178CHMP4bhSnf7-2dJ553F4.4Shax1Chromatin-modifying protein 4bVacuolar protein sorting-associated protein 32-2SNF7 homolog associated with Alix 1CTPP3CTRCT31CHMP4A

Not applicable: no drugs directly targeting CHMP4B are approved. For research compounds: hypothesized disruption of ESCRT-III polymerization or inhibition of protein-protein interactions needed for vesicle scission and viral budding.