AI Article Synopsis
- UBE2C is an essential enzyme in the ubiquitin-proteasome system, necessary for the degradation of proteins like mitotic cyclins and securin, which are crucial for cell division.
- The enzyme has a conserved core for binding with E1 and E3 enzymes and an N-terminal extension that regulates its activity through an inhibitory mechanism.
- High levels of UBE2C are linked to poor cancer prognosis, as it promotes cell proliferation and tumor formation, leading to chromosome instability in transgenic mice.
Article 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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| http://dx.doi.org/10.1016/j.biocel.2013.11.023 | DOI Listing |
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