Tribbles: novel regulators of cell function; evolutionary aspects

Cell Mol Life Sci. 2006 Jul;63(14):1632-41. doi: 10.1007/s00018-006-6007-9.

Abstract

Identification of rate-limiting steps or components of intracellular second messenger systems holds promise to effectively interfere with these pathways under pathological conditions. The emerging literature on a recently identified family of signalling regulator proteins, called tribbles gives interesting clues for how these proteins seem to link several 'independent' signal processing systems together. Via their unique way of action, tribbles co-ordinate the activation and suppression of the various interacting signalling pathways and therefore appear to be key in determining cell fate while responding to environmental challenges. This review summarises our current understanding of tribbles function and also provides an evolutionary perspective on the various tribbles genes.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Autoimmune Diseases / physiopathology
  • Biological Evolution
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / physiology*
  • Cell Lineage
  • Consensus Sequence
  • Drosophila Proteins / chemistry
  • Drosophila Proteins / deficiency
  • Drosophila Proteins / genetics
  • Drosophila Proteins / physiology
  • Drosophila melanogaster / embryology
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / physiology
  • Embryonic Development / genetics
  • Embryonic Development / physiology
  • Evolution, Molecular*
  • Expressed Sequence Tags
  • Gene Expression Regulation / genetics
  • Gene Expression Regulation / physiology
  • Humans
  • Intracellular Signaling Peptides and Proteins / chemistry
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / physiology*
  • Invertebrates / genetics
  • Invertebrates / physiology
  • Molecular Sequence Data
  • Morphogenesis / genetics
  • Morphogenesis / physiology*
  • Neoplasms / physiopathology
  • Protein Kinases / physiology
  • Protein Serine-Threonine Kinases / chemistry
  • Protein Serine-Threonine Kinases / deficiency
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / physiology*
  • Protein Structure, Tertiary
  • Protein Tyrosine Phosphatases / physiology
  • Repressor Proteins / chemistry
  • Repressor Proteins / genetics
  • Repressor Proteins / physiology*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Signal Transduction / genetics
  • Signal Transduction / physiology*
  • Species Specificity
  • Starvation / physiopathology
  • Vertebrates / genetics
  • Vertebrates / physiology
  • Xenopus / physiology
  • Xenopus Proteins / physiology

Substances

  • Cell Cycle Proteins
  • Drosophila Proteins
  • Intracellular Signaling Peptides and Proteins
  • Repressor Proteins
  • TRIB1 protein, human
  • TRIB2 protein, Xenopus
  • TRIB3 protein, human
  • Xenopus Proteins
  • trbl protein, Drosophila
  • Protein Kinases
  • Protein Serine-Threonine Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • TRIB2 protein, human
  • Protein Tyrosine Phosphatases
  • stg protein, Drosophila