From the article: “The endoplasmic reticulum (ER) is the site at which secreted proteins (such as the hormone insulin) and membrane-bound proteins are folded. ATP-dependent chaperones within the ER help proteins fold. This study describes how two key ER chaperones, BiP and Grp94, work together at a molecular level. BiP binds to Grp94, which enables Grp94 to change conformation and hydrolyze ATP. In short, BiP provides a signal to switch on Grp94 conformational changes that are required to help other proteins fold. This finding helps explain how two chaperones can work together collaboratively in protein folding. Because BiP and Grp94 are members of highly conserved chaperone families, these findings may provide insight into chaperone-assisted protein folding beyond the ER.” This project was a collaboration with members of Timothy Street‘s lab in the Brandeis Biochemistry Department.10.1073/pnas.2118793119
Huang B., et al., The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94.
PNAS 119, e2118793119 (2022)