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Charged multivesicular body protein 1B (CHMP1B) is a peripheral membrane-associated structural protein and a member of the ESCRT-III complex, which mediates the formation of multivesicular bodies (MVBs) within the endosomal compartment[1][4][5]. The ESCRT-III pathway controls the invagination and fission of the endosomal limiting membrane, essential for the degradation of internalized membrane proteins, receptor downregulation, lysosomal targeting, and viral budding[1][3][4]. CHMP1B plays a specific role in midbody abscission during cytokinesis by recruiting the microtubule-severing enzyme spastin[3] and is also implicated in chromatin modification through its protein family associations[1][4][6]. Mutations in CHMP1B are linked to pontocerebellar hypoplasia syndromes, likely due to defects in vesicular trafficking and neural development[1]. CHMP1B is not known to be directly targeted by drugs or used as a clinical biomarker, but it is essential for fundamental cellular processes related to protein trafficking, degradation, and cell division[1][3][4][5].
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