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

Fingerprint

TNF Receptor-Associated Factor 4
Tight Junctions
Tumor Necrosis Factor Receptor-Associated Peptides and Proteins
Carcinoma
Epithelium
Carcinogenesis
Proteins
Lipids
Eukaryotic Cells
Epithelial Cells
Cell Membrane
Neoplasms

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

Cite this

Rousseau, Adrien ; Tomasetto, Catherine ; Alpy, Fabien. / TRAF4, une protéine à facettes multiples impliquée dans la progression des carcinomes⋆. In: Biologie Aujourd'hui. 2014 ; Vol. 208, No. 4. pp. 299-310.
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year = "2014",
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TRAF4, une protéine à facettes multiples impliquée dans la progression des carcinomes⋆. / Rousseau, Adrien; Tomasetto, Catherine; Alpy, Fabien.

In: Biologie Aujourd'hui, Vol. 208, No. 4, 2014, p. 299-310.

Research output: Contribution to journalArticle

TY - JOUR

T1 - TRAF4, une protéine à facettes multiples impliquée dans la progression des carcinomes⋆

AU - Rousseau, Adrien

AU - Tomasetto, Catherine

AU - Alpy, Fabien

N1 - © Société de Biologie, 2015.

PY - 2014

Y1 - 2014

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AB - 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.

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Binding Sites

KW - Carcinoma/metabolism

KW - Cell Compartmentation

KW - Cell Movement

KW - Cell Polarity/physiology

KW - Conserved Sequence

KW - Disease Progression

KW - Epithelial Cells/pathology

KW - Epithelial-Mesenchymal Transition

KW - Humans

KW - Membrane Lipids/metabolism

KW - Membrane Proteins/metabolism

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Multigene Family

KW - Neoplasm Proteins/physiology

KW - Phosphatidylinositol Phosphates/metabolism

KW - Protein Conformation

KW - Sequence Alignment

KW - Sequence Homology, Amino Acid

KW - Signal Transduction/physiology

KW - TNF Receptor-Associated Factor 4/genetics

KW - Tight Junctions/physiology

KW - Transforming Growth Factor beta/physiology

KW - Tumor Necrosis Factor Receptor-Associated Peptides and Proteins/chemistry

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VL - 208

SP - 299

EP - 310

JO - Biologie Aujourd'hui

JF - Biologie Aujourd'hui

SN - 2105-0678

IS - 4

ER -