Identification of redox- and glucose-sensitive Txnip interacting proteins using BioID (1153.14)

Many cell signaling processes are dependent on redox-dependent interactions through the thioredoxin (Trx) family. Thioredoxins regulate the reduction-oxidation state of protein substrates through antioxidant enzymatic activities. Thioredoxins have a conserved catalytic site that undergoes reversible oxidation to cysteine disulfide through the transfer of reducing equivalents from the catalytic site cysteine residues to a disulfide substrate. While Txnip has been identified as a critical modulator of several disease pathologies, including β-cell death during hyperglycemia, cardiac hypertrophy, and bronchopulmonary dysplasia, the molecular mechanisms underlying these processes are relatively unknown. The objective of these studies was to establish a cell model to identify Txnip interacting proteins in an effort to understand molecular events underlying the aforementioned disease pathologies. A proximity-based biotin-dependent labeling system (called BioID) was fused to Txnip and stably-transfected into HEK2...