The functions and effects of CUL3-E3 ligases mediated non-degradative ubiquitination

Fengguang Zhai; Jingyun Li; Meng Ye; Xiaofeng Jin

doi:10.1016/j.gene.2022.146562

The functions and effects of CUL3-E3 ligases mediated non-degradative ubiquitination

Gene. 2022 Jul 20:832:146562. doi: 10.1016/j.gene.2022.146562. Epub 2022 May 14.

Authors

Fengguang Zhai¹, Jingyun Li¹, Meng Ye², Xiaofeng Jin³

Affiliations

¹ The Affiliated Hospital of Medical School, Ningbo University, Ningbo 315020, China; Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathphysiology, Medical School of Ningbo University, Ningbo 315211, China.
² The Affiliated Hospital of Medical School, Ningbo University, Ningbo 315020, China; Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathphysiology, Medical School of Ningbo University, Ningbo 315211, China. Electronic address: yemeng@nbu.nbu.edu.cn.
³ The Affiliated Hospital of Medical School, Ningbo University, Ningbo 315020, China; Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathphysiology, Medical School of Ningbo University, Ningbo 315211, China. Electronic address: jinxiaofeng@nbu.edu.cn.

PMID: 35580799
DOI: 10.1016/j.gene.2022.146562

Abstract

Ubiquitination of substrates usually have two fates: one is degraded by 26S proteasome, and the other is non-degradative ubiquitination modification which is associated with cell cycle regulation, chromosome inactivation, protein transportation, tumorigenesis, achondroplasia, and neurological diseases. Cullin3 (CUL3), a scaffold protein, binding with the Bric-a-Brac-Tramtrack-Broad-complex (BTB) domain of substrates recognition adaptor and RING-finger protein 1 (RBX1) form ubiquitin ligases (E3). Based on the current researches, this review has summarized the functions and effects of CUL3-E3 ligases mediated non-degradative ubiquitination.

Keywords: Cullin3; Non-degradative; Ubiquitin ligases; Ubiquitination.

Publication types

Review

MeSH terms

Cullin Proteins* / genetics
Cullin Proteins* / metabolism
Protein Structure, Tertiary
Ubiquitin / metabolism
Ubiquitin-Protein Ligases* / metabolism
Ubiquitination

Substances

Cullin Proteins
Ubiquitin
Ubiquitin-Protein Ligases