Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival

Martin Schwickart, XiaoDong Huang, Jennie R. Lill, Jinfeng Liu, Ronald Ferrando, Dorothy M. French, Heather Maecker, Karen O’Rourke, Fernando Bazan, Jeffrey Eastham-Anderson, Peng Yue, David Dornan, David C. S. Huang and Vishva M. Dixit ()
Additional contact information
Martin Schwickart: Department of Physiological Chemistry,
XiaoDong Huang: Department of Physiological Chemistry,
Jennie R. Lill: Department of Protein Chemistry,
Jinfeng Liu: Department of Bioinformatics,
Ronald Ferrando: Department of Pathology,
Dorothy M. French: Department of Pathology,
Heather Maecker: Department of Translational Oncology,
Karen O’Rourke: Department of Physiological Chemistry,
Fernando Bazan: Department of Protein Engineering,
Jeffrey Eastham-Anderson: Department of Pathology,
Peng Yue: Department of Bioinformatics,
David Dornan: Genentech, Inc., 1 DNA Way, South San Francisco, California 94080, USA
David C. S. Huang: The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia
Vishva M. Dixit: Department of Physiological Chemistry,

Nature, 2010, vol. 463, issue 7277, 103-107

Abstract: Deubiquitinase USP9X stabilizes MCLl The induced myeloid leukaemia cell-differentiation protein MCL1 is often overexpressed in tumours, where it promotes cancer cell survival. Schwickart et al. now show that the deubiquitinase USP9X stabilizes MCLl and is itself often overexpressed in cancer. In multiple myelomas, higher levels of USP9X are associated with poorer prognosis. RNAi knockdown of USP9X in human embryonic kidney 293 cells promotes MCLl degradation and sensitizes cells to anticancer compounds that induce apoptosis, suggesting that targeting USP9X may represent a novel therapeutic strategy for tumours with MCLl overexpression.

Date: 2010
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DOI: 10.1038/nature08646

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