[Identification A novel protein TRIM38 that activate NF-kappaB signaling pathways]

Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi. 2011 Feb;25(1):60-2.
[Article in Chinese]

Abstract

Objective: The tripartite motif (TRIM) proteins are a family of more than 70 human members, however only a few of them have been well studied. It has been shown that TRIM proteins are involved in various cellular processes such as cell proliferation, differentiation, apoptosis and antiviral defense. The functions of TRIM38 are largely unknown. In this study we explore the effect of TRIM38 on NF-kappaB signaling pathway.

Methods: 293T cells were transfected with NF-kappaB-Luc and plasmids expressing TRIM38 and its mutants fused to Flag. 24 h after transfection, cells were harvested and luciferase activities were measured. Data are representative of three independent experiments with triplicate samples. The expression of proteins was analyzed by Western Blot.

Results: TRIM38 could activate NF-kappaB signaling pathway. The mutants of TRIM38 affected the function of TRIM38. Only the mutant of SPRY domain deletion had no obviously influence of the function of TRIM38.

Conclusion: Our study reveals that NF-kappaB is activated in response to TRIM38.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins
  • Cells, Cultured
  • Humans
  • NF-kappa B / physiology*
  • Proteins / physiology*
  • Signal Transduction / physiology*
  • Tripartite Motif Proteins
  • Ubiquitin-Protein Ligases

Substances

  • Carrier Proteins
  • NF-kappa B
  • Proteins
  • Tripartite Motif Proteins
  • TRIM38 protein, human
  • Ubiquitin-Protein Ligases