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Essential Role of hIST1 in Cytokinesis

Agromayor, M; Carlton, JG; Phelan, JP; Matthews, DR; Carlin, LM; Ameer-Beg, S; Bowers, K; (2009) Essential Role of hIST1 in Cytokinesis. MOL BIOL CELL , 20 (5) 1374 - 1387. 10.1091/mbc.E08-05-0474.

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Abstract

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.

Type: Article
Title: Essential Role of hIST1 in Cytokinesis
DOI: 10.1091/mbc.E08-05-0474
Keywords: IMMUNODEFICIENCY-VIRUS TYPE-1, YEAST SACCHAROMYCES-CEREVISIAE, ESCRT-III RECOGNITION, LATE-BUDDING DOMAINS, AAA-ATPASE VPS4, MULTIVESICULAR BODY, STRUCTURAL BASIS, MIT DOMAIN, MEMBRANE ASSOCIATION, PROTEIN INTERACTIONS
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
UCL > Provost and Vice Provost Offices > UCL BEAMS
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Engineering Science
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Engineering Science > Dept of Security and Crime Science
URI: http://discovery.ucl.ac.uk/id/eprint/174391
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