Allosteric regulation of the tyrosine phosphatase PTP1B by a protein-protein interaction.

ABSTRACT: The rapid identification of protein-protein interactions has been significantly enabled by mass spectrometry (MS) proteomics-based methods, including affinity purification-MS, crosslinking-MS, and proximity-labeling proteomics. While these methods can reveal networks of interacting proteins, they cannot reveal how specific protein-protein interactions alter protein function or cell signaling. For instance, when two proteins interact, there can be emergent signaling processes driven purely by the individual activities of those proteins being co-localized. Alternatively, protein-protein interactions can allosterically regulate function, enhancing or suppressing activity in response to binding. In this work, we investigate the interaction between the tyrosine phosphatase PTP1B and the adaptor

SUBMITTER: Chartier CA 

PROVIDER: S-EPMC11275736 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature