Tribbles: A family of kinase-like proteins with potent signalling regulatory function

The recent identification of tribbles as regulators of signal processing systems and physiological processes, including development, together with their potential involvement in diabetes and cancer, has generated considerable interest in these proteins. Tribbles have been reported to regulate activa...

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Bibliographic Details
Published in:Cellular signalling 2007-02, Vol.19 (2), p.238-250
Main Authors: Hegedus, Z., Czibula, A., Kiss-Toth, E.
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Animals
Apoptosis Regulatory Proteins - genetics
Apoptosis Regulatory Proteins - metabolism
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Conserved Sequence
Drosophila Proteins - genetics
Drosophila Proteins - metabolism
Evolution, Molecular
Humans
Models, Biological
Molecular Sequence Data
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Phosphotransferases - genetics
Protein Kinases - metabolism
Protein Structure, Tertiary
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Sequence Homology, Amino Acid
Signal Transduction
Tribbles
Tribbles proteins
Xenopus Proteins - metabolism
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Summary:The recent identification of tribbles as regulators of signal processing systems and physiological processes, including development, together with their potential involvement in diabetes and cancer, has generated considerable interest in these proteins. Tribbles have been reported to regulate activation of a number of intracellular signalling pathways with roles extending from mitosis and cell activation to apoptosis and modulation of gene expression. The current review summarises our current understanding of interactions between tribbles and various other proteins. Since our understanding on the molecular basis of tribbles function is far from complete, we also describe a bioinformatic analysis of various segments of tribbles proteins, which has revealed a number of highly conserved peptide motifs with potentially important functional roles.
ISSN:0898-6568
1873-3913
DOI:10.1016/j.cellsig.2006.06.010