CHMP7 (charged multivesicular body protein 7) is an ESCRT-III-like protein that plays critical roles in nuclear envelope maintenance and membrane repair. Its primary function involves recruiting ESCRT-III complexes to the nuclear envelope during late anaphase, where it collaborates with SPAST to promote nuclear envelope sealing and mitotic spindle disassembly 1. CHMP7 is recruited to the reforming nuclear envelope by LEMD2 through direct binding interactions 12. The protein forms co-oligomeric rings with LEM2 to create macromolecular seals at the confluence of membranes, chr8, and spindle structures 2. In pathological conditions, CHMP7 dysfunction contributes significantly to neurodegenerative diseases. Nuclear accumulation of CHMP7 initiates nuclear pore complex injury, leading to nucleoporin alterations and subsequent TDP-43 dysfunction in both sporadic and familial ALS 3. This pathological process is promoted by CHMP2B and can be triggered by RNA splicing inhibition 45. Additionally, reactive oxygen species can disrupt CHMP7's normal function in micronuclei, promoting noncanonical oligomerization and membrane disruption that leads to chromosome 8 6. CHMP7 variants have also been validated as ADHD risk factors, with reduced expression causing hyperactivity and smaller brain volumes in zebrafish models 7.