RNF13 (PA-TM-RING RNFprotein)

3.2. Cell Proliferation and Differentiation

RNF13,

a member of the PA-TM-RING family, appears to be associated with cell proliferation, differentiation and tumorigenesis [30].
RNF13 was found to be highly expressed in chicken skeletal myoblasts [124].
The expression of RNF13 gradually decreases during skeletal myogenesis, and is upregulated by myostatin, a myogenesis negative regulator. Overexpression of RNF13 inhibits skeletal muscle proliferation in a manner that is dependent on its E3 activity. Thus, RNF13 may contribute to myogenesis as a negative regulator of cell proliferation. In addition, RNF13 expression is increased in differentiating rat B35 neuroblastoma cells, and overexpression of RNF13 promotes neurite extension in rat PC12 pheochromocytoma cells, suggesting an involvement of RNF13 in neuronal development [125].
High-level expression of RNF13 is also observed in pancreatic ductal adenocarcinoma as well as in precancerous pancreatic lesions,..
RNF13 has been reported to be localized to various membrane structures, including the nucleus, ER, Golgi apparatus and endosomes. Recent studies have reported that RNF13 is present in the endosomal and lysosomal compartments, and the C-terminal region containing the RNF domain is released into the cytosol by proteolytic cleavage [125].
Activation of protein kinase C inhibits this cleavage and stabilizes the full-length RNF13 [127].
The stabilized RNF13 is then transported to the inner nuclear membrane via the recycling endosomes, thereby exposing its RNF domain to the nucleoplasm. RNF13 may modulate gene expression and signal transduction by mediating ubiquitination in response to various stimuli [35,127].
 It is imperative to identify the RNF13 substrate proteins to obtain a better understanding of the physiological role and mechanism of action of RNF13
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4021871/
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