Ubiquitin-conjugating enzyme E2C: A potential cancer biomarker |
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| Institution: | 1. School of Science and Health, The University of Western Sydney, Australia;2. Central Clinical School and Bosch Institute, The University of Sydney and Department of Endocrinology, Royal Prince Alfred Hospital, Sydney, Australia;3. The Kinghorn Cancer Centre & Cancer Division, Garvan Institute of Medical Research, Sydney, Australia;4. St Vincent''s Clinical School, Faculty of Medicine, University of New South Wales, Sydney, Australia;1. Leeds Institute for Data Analytics, University of Leeds, United Kingdom;2. Department of Medicine, University of Toronto, Canada;1. Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, United States;2. Department of Pharmacology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, United States |
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| Abstract: | The ubiquitin-conjugating enzymes 2C (UBE2C) is an integral component of the ubiquitin proteasome system. UBE2C consists of a conserved core domain containing the catalytic Cys residue and an N-terminal extension. The core domain is required for ubiquitin adduct formation by interacting with the ubiquitin-fold domain in the E1 enzyme, and contributes to the E3 enzyme binding. UBE2C N-terminal extension regulates E3 enzyme activity as a part of an intrinsic inhibitory mechanism. UBE2C is required for the destruction of mitotic cyclins and securin, which are essential for spindle assembly checkpoint and mitotic exit. The UBE2C mRNA and/or protein levels are aberrantly increased in many cancer types with poor clinical outcomes. Accumulation of UBE2C stimulates cell proliferation and anchorage-independent growth. UBE2C transgenic mice are prone to develop spontaneous tumors and carcinogen-induced tumor with evidence of chromosome aneuploidy. |
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| Keywords: | Ubiquitin-conjugating enzymes 2C Anaphase-promoting complex Ubiquitination Cancer |
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