TRAF4, une protéine à facettes multiples impliquée dans la progression des carcinomes⋆

Translated title of the contribution: TRAF4, a multifaceted protein involved in carcinoma progression

Adrien Rousseau, Catherine Tomasetto, Fabien Alpy

Research output: Contribution to journalArticle

Abstract

Eukaryotic epithelial cells form a sheet of contiguous cells, called epithelium, by means of the establishment of well-developed junctional complexes. These junctional complexes ensure the cell cohesion in the tissue and separate the plasma membrane into an apical and a basolateral compartment. This apicobasal polarity, which is crucial for both the architecture and the function of epithelia, is mainly maintained by tight junctions (TJS). Indeed, TJS weakening or loss disrupts the integrity of the epithelium, a process participating to the formation and progression of carcinomas. It has recently been shown that TRAF4, a protein dynamically localized in TJS and commonly overexpressed in carcinomas, plays a variety of functions in tumor progression. Here, we review recent data implicating TRAF4 in carcinogenesis. First, the conserved TRAF proteins family will be presented, and then the molecular mechanism addressing TRAF4 to TJS which involves lipid binding by the TRAF domain will be described. The various roles of TRAF4 in carcinogenesis will be discussed. Finally, we will highlight the ability of all TRAF proteins to bind lipids and discuss its potential functional relevance.

Original languageFrench
Pages (from-to)299-310
Number of pages12
JournalBiologie Aujourd'hui
Volume208
Issue number4
DOIs
Publication statusPublished - 2014

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Keywords

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Binding Sites
  • Carcinoma/metabolism
  • Cell Compartmentation
  • Cell Movement
  • Cell Polarity/physiology
  • Conserved Sequence
  • Disease Progression
  • Epithelial Cells/pathology
  • Epithelial-Mesenchymal Transition
  • Humans
  • Membrane Lipids/metabolism
  • Membrane Proteins/metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Multigene Family
  • Neoplasm Proteins/physiology
  • Phosphatidylinositol Phosphates/metabolism
  • Protein Conformation
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Signal Transduction/physiology
  • TNF Receptor-Associated Factor 4/genetics
  • Tight Junctions/physiology
  • Transforming Growth Factor beta/physiology
  • Tumor Necrosis Factor Receptor-Associated Peptides and Proteins/chemistry

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