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Vol. 20, Issue 5, 1374-1387, March 1, 2009

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Essential Role of hIST1 in Cytokinesis

Monica Agromayor^*, Jez G. Carlton^*, John P. Phelan, Daniel R. Matthews, Leo M. Carlin, Simon Ameer-Beg, Katherine Bowers, and Juan Martin-Serrano^*

*Department of Infectious Diseases, King's College London School of Medicine, London SE1 9RT, United Kingdom; The Richard Dimbleby Department of Cancer Research and The Randall Division of Cell and Molecular Biophysics, King's College London School of Medicine, London SE1 9RT, United Kingdom; and Institute of Structural and Molecular Biology, Division of Biosciences, University College London, London WC1E 6BT, United Kingdom

Submitted May 13, 2008; Revised November 13, 2008; Accepted December 23, 2008
Monitoring Editor: Stephen Doxsey

The last steps of multivesicular body (MVB) formation, human immunodeficiency virus (HIV)-1 budding and cytokinesis require a functional endosomal sorting complex required for transport (ESCRT) machinery to facilitate topologically equivalent membrane fission events. Increased sodium tolerance (IST) 1, a new positive modulator of the ESCRT pathway, has been described recently, but an essential function of this highly conserved protein has not been identified. Here, we describe the previously uncharacterized KIAA0174 as the human homologue of IST1 (hIST1), and we report its conserved interaction with VPS4, CHMP1A/B, and LIP5. We also identify a microtubule interacting and transport (MIT) domain interacting motif (MIM) in hIST1 that is necessary for its interaction with VPS4, LIP5 and other MIT domain-containing proteins, namely, MITD1, AMSH, UBPY, and Spastin. Importantly, hIST1 is essential for cytokinesis in mammalian cells but not for HIV-1 budding, thus providing a novel mechanism of functional diversification of the ESCRT machinery. Last, we show that the hIST1 MIM activity is essential for cytokinesis, suggesting possible mechanisms to explain the role of hIST1 in the last step of mammalian cell division.

Address correspondence to: Juan Martin-Serrano (juan.martin_serrano{at}kcl.ac.uk)

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