RNF157 (Ring finger protein 157) is highly involved in the regulation of neuronal development and morphology of the neurons. It promotes dendritic growth by interacting with adaptor protein Fe65. Its N-terminal end binds to the second PTB domain of Fe65 to ubiquitinate Fe65 via E3 ligase activity. It has also been reported that RNF157 may be involved in the regulation of membrane protein trafficking.
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Age-related cataract (ARC) is a major cause of vision impairment worldwide. The E3 ubiquitin ligase RING finger protein 157 (RNF157) is involved in regulating cell survival and downregulated in human cataractous lens samples. However, the function of RNF157 in cataracts
Plant LOSS OF GDU 2 (LOG2) and Mammalian Mahogunin Ring Finger 1 (MGRN1) proteins are RING-type E3 ligases sharing similarity N-terminal to the RING domain. Deletion of this region disrupts the interaction of LOG2 with the plant membrane protein GLUTAMINE
Cell death and differentiation, 22(4), 626-642 (2014-10-25)
Neuronal health is essential for the long-term integrity of the brain. In this study, we characterized the novel E3 ubiquitin ligase ring finger protein 157 (RNF157), which displays a brain-dominant expression in mouse. RNF157 is a homolog of the E3
Frontiers in oncology, 12, 1021270-1021270 (2022-10-21)
Exosomes have been identified to mediate the transmission of RNAs among different cells in tumor microenvironment, thus affecting the progression of different diseases. However, exosomal messenger RNAs (mRNAs) have been rarely explored. RNF157 mRNA has been found to be up-regulated
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