Source: Society for Experimental Biology and Medicine | Summary: Protein ubiquitination is known to result in its proteasomal degradation or to serve as a signal for tissue-specific cellular functions. Here it is reported that mice with a mutant form of the E3 ubiquitin ligase ITCH display reduced litter sizes due to a maternal effect. Mutant females had decreased numbers of implantations, corpa lutea, and extended estrous cycles. The results indicate for the first time that loss of functional ITCH disrupts female reproduction.
"The post-translational addition of ubiquitin to proteins by enzymes of the E3 ubiquitin ligase family is largely recognized as a means to target misfolded or unwanted proteins for degradation by the proteasome.
However, it is now understood that ubiquitination serves as a signal to modify a number of cellular functions such as protein trafficking, cell signaling, DNA repair, chromatin modifications, cell-cycle progression, and cell death.
Though these functions are integral for all cells throughout the body, the physiologic role of specific E3 ligases must yet be defined in the context of various tissues. For example, very few studies exist that interrogate the function of specific E3 ubiquitin ligases in the reproductive system..."
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https://www.sciencedaily.com/releases/2016/02/160229182656.htm
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