RNF13: an emerging RING finger ubiquitin ligase important in cell proliferation

Protein ubiquitination mediated by ubiquitin ligases plays a very important role in a wide spectrum of biological processes including development and disease pathogenesis. RING finger protein 13 (RNF13) is a recently identified ubiquitin ligase which contains an N‐terminal protease‐associated domain...

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Bibliographic Details
Published in:The FEBS journal 2011-01, Vol.278 (1), p.78-84
Main Authors: Jin, Xianglan, Cheng, He, Chen, Jie, Zhu, Dahai
Format: Article
Language:English
Subjects:
Amino Acid Sequence
cancer
Cell adhesion & migration
Cell Proliferation
development
differentiation
E3 ubiquitin ligase
Gene Expression Regulation, Enzymologic
Humans
Molecular Sequence Data
muscle development
myogenesis
neoplasms
neurogenesis
pathogenesis
proliferation
Proteins
RING finger domain
RING Finger Domains
RNF13
Sequence Alignment
ubiquitin-protein ligase
Ubiquitin-Protein Ligases - metabolism
ubiquitination
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Summary:Protein ubiquitination mediated by ubiquitin ligases plays a very important role in a wide spectrum of biological processes including development and disease pathogenesis. RING finger protein 13 (RNF13) is a recently identified ubiquitin ligase which contains an N‐terminal protease‐associated domain and a C‐terminal RING finger domain separated by a transmembrane region. RNF13 is an evolutionarily conserved protein. Most interestingly, RNF13 expression is developmentally regulated during myogenesis and is upregulated in various human tumors. These data suggest that RNF13, acting as an ubiquitin ligase, might have profound biological functions during development and disease. This minireview summarizes recent work on RNF13 functions related to cell proliferation, differentiation and cancer development.
ISSN:1742-464X
1742-4658
DOI:10.1111/j.1742-4658.2010.07925.x