Spatially resolved profiling of protein conformation and interactions by biocompatible chemical cross-linking in living cells.

ABSTRACT: Unlocking the intricacies of protein structures and interactions within the dynamic landscape of subcellular organelles presents a significant challenge. To address this, we introduce SPACX, a method for spatially resolved protein complex profiling via biocompatible chemical cross(x)-linking with subcellular isolation, designed to monitor protein conformation, interactions, and translocation in living cells. By rapidly capturing protein complexes in their native physiological state and efficiently enriching cross-linked peptides, SPACX allows comprehensive analysis of the protein interactome within living cells. Leveraging structure refinement with cross-linking restraints, we identify subcellular-specific conformation heterogeneity of PTEN, revealing dynamic differences in its dual specif

SUBMITTER: Zhao L 

PROVIDER: S-EPMC11436894 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature