Advanced Search

Submit Manuscript

Volume 24, No 6, Jun 2014

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 24 Issue 6, June 2014: 762-765   |  Open Access

LETTERS TO THE EDITOR

Structural insights into the TRIM family of ubiquitin E3 ligases

Yang Li1,2,*, Han Wu1,2,*, Wei Wu3,*, Wei Zhuo1,2,*, Weixiao Liu4, Yixiao Zhang1, Minzhang Cheng1,2, Ye-Guang Chen1,2, Ning Gao1, Hongtao Yu5, Linfang Wang3, Wei Li4 and Maojun Yang1,2

1MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China
2Department of Pharmacology and Pharmaceutical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China
3State Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, Peking Union Medical College, Tsinghua University, Beijing 100005, China
4State Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China
5Howard Hughes Medical Institute, Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA
Correspondence: Maojun Yang, Tel: +86-10-6278-9400; Fax: +86-10-6279-2736 E-mail: maojunyang@tsinghua.edu.cn; Wei Li, Tel: +86-10-6480-7529; Fax: +86-10-6480-7529 E-mail: leways@ioz.ac.cn; Linfang Wang, Tel: +86-10-6224-0803; Fax: +86-10-6224-0529(wang.linfang@imicams.ac.cn)

TRIM proteins play important roles in a wide range of biological processes, including cell proliferation, differentiation, development, apoptosis, oncogenesis and innate immunity1,2. The N-terminal regions of all TRIM proteins contain a RING finger domain followed by one or two B-box domains and a coiled-coil domain (CCD). The RING-finger domain comprises conserved cysteine and histidine residues that bind two zinc atoms in a 'cross-brace' arrangement, and is essential for recruiting the ubiquitin-charged ubiquitin-conjugating enzymes (E2~Ub). The B-box domains, differing in both the number and spacing of the conserved cysteine and histidine residues3, are typically composed of B1 and B2 domains, but some TRIM members only contain a B2 domain. CCD following the B-box domains has been proposed to mediate protein-protein interactions, particularly homomeric and heteromeric interactions by forming intertwining helices among TRIM family and other proteins4,5.


10.1038/cr.2014.46

FULL TEXT | PDF

Browse 2412