Tribbles homolog 3 is a protein that in humans is encoded by the TRIB3 gene. [5] [6] [7]
Tribbles homolog 3 is a protein that in humans is encoded by the TRIB3 gene. [5] [6] [7]
The protein encoded by this gene is a putative protein kinase that is induced by the transcription factor NF-kappaB. It is a pseudoenzyme that is thought to be a negative regulator of NF-kappaB, and can also sensitize cells to TNF- and TRAIL-induced apoptosis. In addition, this protein has been reported to negatively regulate the cell survival serine-threonine kinase AKT1. [7] TRIB3 has recently been associated with neuronal signalling, and like TRIB1 and TRIB2, could be considered as a potential allosteric drug target. [8] [9]
TRIB3 has been shown to interact with:
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Tribbles homolog 1 is a protein kinase that in humans is encoded by the TRIB1 gene. Orthologs of this protein pseudokinase (pseudoenzyme) can be found almost ubiquitously throughout the animal kingdom. It exerts its biological functions through binding to signalling proteins of the MAPKK level of the MAPK pathway, therefore eliciting a regulatory role in the function of this pathway which mediates proliferation, apoptosis and differentiation in cells. Tribbles-1 is encoded by the trib1 gene, which in humans can be found on chromosome 8 at position 24.13 on the longest arm (q). Recent crystal structures show that Tribbles 1 has an unusual 3D structure, containing a 'broken' C-helix region, a binding site for ubiquitinated substrates such as C/EBPalpha and a key regulatory C-tail region. Like TRIB2 and TRIB3, TRIB1 has recently been considered as a potential allosteric drug target.
Tribbles homolog 2 is an atypical protein kinase that is encoded in human by the TRIB2 gene. TRIB2 is a pseudokinase member of the (pseudoenzyme) class of signaling/scaffold proteins, possessing very low vestigial catalytic output in vitro and critical scaffolding signaling functions in cells. It is known to signal to canonical MAPK and AKT pathways and to regulate the ubiquitination of substrates with important functions in cell proliferation that control the cell ccyle. It has also been associated with various diseases, especially in human and murine blood and solid tumor models. Like TRIB1 and TRIB3, TRIB2 has recently been considered as a potential allosteric drug target, and its three dimensional structure has been solved with the aid of stabilizing nanobodies corroborating the potential for new approaches for drug targeting outside the highly degraded ATP site and is a putative regulator of cancer-associated signalling and survival through AKT pSer473 modulation. Recent work has established a convincing link between targetable overexpression of TRIB2 and prostate cancer drug responses
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