Autophagy is a mechanism of cellular self-degradation that is very important for cellular homeostasis and differentiation. Components of the endosomal sorting complex required for transport (ESCRT) machinery are required for endosomal sorting and also for autophagy and the completion of cytokinesis. Here we show that the ESCRT-III subunit CHMP4B not only localizes to normal cytokinetic bridges but also to chromosome bridges and micronuclei, the latter surrounded by lysosomes and autophagosomes. Moreover, CHMP4B can be co-immunoprecipitated with chromatin. Interestingly, a CHMP4B mutation associated with autosomal dominant posterior polar cataract abolishes the ability of CHMP4B to localize to micronuclei. We propose that CHMP4B, through its association with chromatin, may participate in the autophagolysosomal degradation of micronuclei and other extranuclear chromatin. This may have implications for DNA degradation during lens cell differentiation, thus potentially protecting lens cells from cataract development.

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autophagolysosomal degradation of micronuclei cytokinetic bridges autophagy escrtiii subunit endosomal sorting complex lens cell differentiation other extranuclear chmp4b chromatin transport polar cataract machinery cellular selfdegradation of cytokinesis dna degradation

Antonia P. Sagona,Harald Stenmark,.Association of CHMP4B and Autophagy with Micronuclei: Implications for Cataract Formation. 2014 (),.

Antonia P. Sagona,Harald Stenmark,"Association of CHMP4B and Autophagy with Micronuclei: Implications for Cataract Formation" 2014

Antonia P. Sagona,Harald Stenmark,"Association of CHMP4B and Autophagy with Micronuclei: Implications for Cataract Formation"