Emerging role of Lys-63 ubiquitination in protein kinase and phosphatase activation and cancer development

Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
Oncogene (Impact Factor: 8.46). 08/2010; 29(32):4493-503. DOI: 10.1038/onc.2010.190
Source: PubMed


Ubiquitination is an important post-translational modification that has a pivotal role in numerous biological functions, such as cell growth, proliferation, apoptosis, DNA damage response, innate immune response and neuron degeneration. Although ubiquitination is thought to achieve these functions by targeting proteins for proteasome-dependent degradation, recent studies suggest that ubiquitination also has nonproteolytic functions, such as protein trafficking, kinase and phosphatase activation, which are involved in cell survival and cancer development. These progresses have advanced our current understanding of the novel functions of ubiquitination in signal transduction pathways and may provide novel paradigms for the treatment of human cancers.

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Available from: Wei-Lei Yang, Nov 12, 2014
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    • "modifications have non-proteolytic functional consequences such as kinase activation, DNA repair, and protein trafficking [9] [10]. Polyubiquitylation involves three distinct and consecutive enzymatic steps (Fig. 1A): ubiquitin activation by an E1 ubiquitinactivating enzyme (UAE), the transfer of the AMP-charged, activated ubiquitin to an E2 ubiquitin-conjugating enzyme (UBC), and the transfer of ubiquitin to the substrate through the activity of an E3 ubiquitin ligase [3–5,8]. "
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