ESCRT-III Governs the Aurora B-Mediated Abscission Checkpoint Through CHMP4C

Jeremy G. Carlton; Anna Caballe; Monica Agromayor; Magdalena Kloc; Juan Martin-Serrano

doi:10.1126/science.1217180

ESCRT-III Governs the Aurora B-Mediated Abscission Checkpoint Through CHMP4C

Infectious Diseases

King's College London

Research output: Contribution to journal › Article › peer-review

264 Citations (Scopus)

Abstract

The endosomal sorting complex required for transport (ESCRT) machinery plays an evolutionarily conserved role in cytokinetic abscission, the final step of cell division where daughter cells are physically separated. Here, we show that charged multivesicular body (MVB) protein 4C (CHMP4C), a human ESCRT-III subunit, is involved in abscission timing. This function correlated with its differential spatiotemporal distribution during late stages of cytokinesis. Accordingly, CHMP4C functioned in the Aurora B-dependent abscission checkpoint to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. CHMP4C engaged the chromosomal passenger complex (CPC) via interaction with Borealin, which suggested a model whereby CHMP4C inhibits abscission upon phosphorylation by Aurora B. Thus, the ESCRT machinery may protect against genetic damage by coordinating midbody resolution with the abscission checkpoint.

Original language	English
Pages (from-to)	220 - 225
Number of pages	6
Journal	Science
Volume	336
Issue number	6078
DOIs	https://doi.org/10.1126/science.1217180
Publication status	Published - 13 Apr 2012

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abstract = "The endosomal sorting complex required for transport (ESCRT) machinery plays an evolutionarily conserved role in cytokinetic abscission, the final step of cell division where daughter cells are physically separated. Here, we show that charged multivesicular body (MVB) protein 4C (CHMP4C), a human ESCRT-III subunit, is involved in abscission timing. This function correlated with its differential spatiotemporal distribution during late stages of cytokinesis. Accordingly, CHMP4C functioned in the Aurora B-dependent abscission checkpoint to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. CHMP4C engaged the chromosomal passenger complex (CPC) via interaction with Borealin, which suggested a model whereby CHMP4C inhibits abscission upon phosphorylation by Aurora B. Thus, the ESCRT machinery may protect against genetic damage by coordinating midbody resolution with the abscission checkpoint.",

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T1 - ESCRT-III Governs the Aurora B-Mediated Abscission Checkpoint Through CHMP4C

AU - Carlton, Jeremy G.

AU - Caballe, Anna

AU - Agromayor, Monica

AU - Kloc, Magdalena

AU - Martin-Serrano, Juan

PY - 2012/4/13

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AB - The endosomal sorting complex required for transport (ESCRT) machinery plays an evolutionarily conserved role in cytokinetic abscission, the final step of cell division where daughter cells are physically separated. Here, we show that charged multivesicular body (MVB) protein 4C (CHMP4C), a human ESCRT-III subunit, is involved in abscission timing. This function correlated with its differential spatiotemporal distribution during late stages of cytokinesis. Accordingly, CHMP4C functioned in the Aurora B-dependent abscission checkpoint to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. CHMP4C engaged the chromosomal passenger complex (CPC) via interaction with Borealin, which suggested a model whereby CHMP4C inhibits abscission upon phosphorylation by Aurora B. Thus, the ESCRT machinery may protect against genetic damage by coordinating midbody resolution with the abscission checkpoint.

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ESCRT-III Governs the Aurora B-Mediated Abscission Checkpoint Through CHMP4C

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