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ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes

Research output: Contribution to journalArticle

Michael A. Hadders, Monica Agromayor, Takayuki Obita, Olga Perisic, Anna Caballe, Magdalena Kloc, Meindert H. Lamers, Roger L. Williams, Juan Martin Serrano

Original languageEnglish
Pages (from-to)17424-17429
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number43
Early online date8 Oct 2012
Publication statusPublished - 23 Oct 2012

King's Authors


The endosomal sorting complexes required for transport (ESCRT) proteins have a critical function in abscission, the final separation of the daughter cells during cytokinesis. Here, we describe the structure and function of a previously uncharacterized ESCRT-III interacting protein, MIT-domain containing protein 1 (MITD1). Crystal structures of MITD1 reveal a dimer, with a microtubule-interacting and trafficking (MIT) domain at the N terminus and a unique, unanticipated phospholipase D-like (PLD) domain at the C terminus that binds membranes. We show that the MIT domain binds to a subset of ESCRT-III subunits and that this interaction mediates MITD1 recruitment to the midbody during cytokinesis. Depletion of MITD1 causes a distinct cytokinetic phenotype consistent with destabilization of the midbody and abscission failure. These results suggest a model whereby MITD1 coordinates the activity of ESCRT-III during abscission with earlier events in the final stages of cell division.

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