Cunard R .

P30 DK063491 NIDDK NIH HHS

Figure 1. The basic protein structure of TRB isoforms. There is significant sequence divergence in the N-terminal domain among tribbles homologs. The pseudokinase domain has what is believed to be a kinase-dead catalytic loop [26], and the C-terminal domain has MEK1 (binds MAPKK, [44]) and COP1 (binds ubiquitin ligases) binding motifs. The pseudokinase domain is important for protein-protein interactions between transcription factors.

Figure 2. TRB3 at the crossroads of ER stress and mTORC function. Acute and chronic kidney disease are associated with activation of the Endoplasmic Reticulum Stress pathway. During ER stress Protein kinase RNA (PKR)-like ER kinase (PERK) phosphorylates eukaryotic translation initiation factor α (eIF2α) and inhibits protein translation. Additionally, there is selective translation of activating transcription factor-4 (ATF4), which induces expression of C/EBP homologous protein (CHOP) and drives TRB3 expression. Kidney disease is also associated with activation of mTORC and inhibition of autophagy flux. We propose that in the kidney, TRB3 binds to Rictor and mTORC2 and inhibits phosphorylation of pAKTSer473. This in turn reduces inflammatory gene expression (IL-6 and MCP-1) and potentially modifies activation of mTORC1 and autophagy.

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