title: Enterovirus 71 induces degradation of TRIM38, a potential E3 ubiquitin ligase.
abstract: BACKGROUND
  The tripartite motif (TRIM) proteins are a family of more than 70 members in human. However, only a few of them have been well studied. The TRIM proteins contain the conserved RING, B-box, coiled-coil, and SPRY domains, most of which are involved in protein ubiquitination. TRIM38 is a member of the TRIM protein family, which we studied in more detail here as its functions are largely unknown.
  
  
  RESULTS
  Our study shows that, similar to other TRIM family members, TRIM38 is localized in the cytoplasm. TRIM38 increases ubiquitination of other cellular proteins and catalyzes self-ubiquitination. TRIM38 also promotes K63- and K48-linked ubiquitination of cellular proteins. An intact RING domain is important for the functions of TRIM38. In addition, enterovirus 71 infection induces TRIM38 degradation.
  
  
  CONCLUSIONS
  Our observations demonstrate that TRIM38 has E3 ubiquitin ligase activity and can be degraded during virus infection. These findings may provide insight into innate immune signaling pathways.
authors.affiliation: State Key Laboratory of Molecular Virology and Genetic Engineering, Institute of Pathogen Biology, Peking Union Medical College & Chinese Academy of Medical Sciences, Beijing 100730, P.R. China.
authors.forename: Xinlei
authors.initials: X
authors.lastname: Liu
authors.forename: Xiaobo
authors.initials: X
authors.lastname: Lei
authors.forename: Zhuo
authors.initials: Z
authors.lastname: Zhou
authors.forename: Zhenmin
authors.initials: Z
authors.lastname: Sun
authors.forename: Qinghua
authors.initials: Q
authors.lastname: Xue
authors.forename: Jianwei
authors.initials: J
authors.lastname: Wang
authors.forename: Tao
authors.initials: T
authors.lastname: Hung
mesh_terms: D000595:Amino Acid Sequence; D002352:Carrier Proteins; D045744:Cell Line, Tumor; D029821:Enterovirus A, Human / Q000502:physiology*; D004769:Enterovirus Infections / Q000201:enzymology* / Q000378:metabolism / Q000821:virology; D006801:Humans; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D000070584:Tripartite Motif Proteins; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D002352:Carrier Proteins; D011506:Proteins; D000070584:Tripartite Motif Proteins; C106984:TRIM38 protein, human; D044767:Ubiquitin-Protein Ligases