Time-Resolved Interactome Profiling Deconvolutes Secretory Protein Quality Control Dynamics

ABSTRACT: Many cellular processes are governed by protein-protein interactions that require tight spatial and temporal regulation. Accordingly, it is necessary to understand the dynamics of these inter-actions to fully comprehend and elucidate cellular processes and pathological disease states. To map de novo protein-protein interactions with time-resolution at an organelle-wide scale we developed a quantitative mass-spectrometry method, time-resolved interactome profiling (TRIP). We apply TRIP to elucidate aberrant protein interaction dynamics that lead to the protein misfold-ing disease congenital hypothyroidism. We deconvolute altered temporal interactions of the thyroid hormone precursor thyroglobulin with pathways implicated in hypothyroidism pathophysiology such as Hsp70/90 assisted folding, d

SUBMITTER: Madison Wright 

PROVIDER: S-SCDT-10_1038-S44320-024-00058-1 | biostudies-other |

REPOSITORIES: biostudies-other