Multifaceted Roles of the E3 Ubiquitin Ligase RING Finger Protein 115 in Immunity and Diseases

Ubiquitination is a post-translational modification that plays essential roles in various physiological and pathological processes. Protein ubiquitination depends on E3 ubiquitin ligases that catalyze the conjugation of ubiquitin molecules on lysine residues of targeted substrates. RING finger prote...

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Bibliographic Details
Published in:Frontiers in immunology 2022-06, Vol.13, p.936579
Main Authors: Wang, Mei-Xia, Liuyu, Tianzi, Zhang, Zhi-Dong
Format: Article
Language:English
Subjects:
antiviral immunity
autoimmunity
Breast Neoplasms
cancers
Cell Proliferation
DNA damage repair
Female
Humans
Immunology
RNF115
Ubiquitin - metabolism
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
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Summary:Ubiquitination is a post-translational modification that plays essential roles in various physiological and pathological processes. Protein ubiquitination depends on E3 ubiquitin ligases that catalyze the conjugation of ubiquitin molecules on lysine residues of targeted substrates. RING finger protein 115 (RNF115), also known as breast cancer associated gene 2 (BCA2) and Rab7-interacting RING finger protein (Rabring7), has been identified as a highly expressed protein in breast cancer cells and tissues. Later, it has been demonstrated that RNF115 catalyzes ubiquitination of a series of proteins to modulate a number of signaling pathways, and thereby regulates viral infections, autoimmunity, cell proliferation and death and tumorigenesis. In this review, we introduce the identification, expression and activity regulation of RNF115, summarize the substrates and functions of RNF115 in different pathways, and discuss the roles of RNF115 as a biomarker or therapeutic target in diseases.
ISSN:1664-3224
1664-3224
DOI:10.3389/fimmu.2022.936579