Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/97735
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Type: Journal article
Title: La FAM fatale: USP9X in development and disease
Author: Murtaza, M.
Jolly, L.
Gecz, J.
Wood, S.
Citation: Cellular and Molecular Life Sciences, 2015; 72(11):2075-2089
Publisher: Springer
Issue Date: 2015
ISSN: 1420-682X
1420-9071
Statement of
Responsibility: 
Mariyam Murtaza, Lachlan A. Jolly, Jozef Gecz, Stephen A. Wood
Abstract: Deubiquitylating enzymes (DUBs), act downstream of ubiquitylation. As such, these post-post-translational modifiers function as the final arbitrators of a protein substrate's ubiquitylation status, thus regulating its fate. In most instances, DUBs moderate the absolute level of a substrate, its locality or activity, rather than being an "all-or-none" phenomenon. Yet, disruption of this quantitative regulation can produce dramatic qualitative differences. The ubiquitin-specific protease 9X (USP9X/FAM) is a substrate-specific DUB, which displays an extraordinarily high level of sequence conservation from Drosophila to mammals. It is primarily the recent revelations of USP9X's pivotal role in human cancers, both as oncogene or tumour suppressor, in developmental disorders including intellectual disability, epilepsy, autism and developmental delay that has led to a subsequent re-examination of its molecular and cellular functions. Results from experimental animal models have implicated USP9X in neurodegeneration, including Parkinson's and Alzheimer's disease, as well as autoimmune diseases. In this review, we describe the current and accumulated knowledge on the molecular, cellular and developmental aspects of USP9X function within the context of the biological consequences during normal development and disease.
Keywords: Ubiquitin; Fat facets; Embryo; Stem cells
Rights: © The Author(s) 2015 Open Access. This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
RMID: 0030023024
DOI: 10.1007/s00018-015-1851-0
Appears in Collections:Medicine publications

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