“…Studies of the ERp29 D. melanogaster orthologue, Wind, have shown that five residues in the CTD of Wind (E212, R215, R218, L219, and L232) contribute to its ability to chaperone the secretory substrate, Pipe, from the ER to the Golgi compartment (1). Furthermore, when fused to the NTD of Wind, the CTD of mouse ERp29 can functionally replace the corresponding Wind domain, and mutations corresponding to the ERp29 CTD residues (E220Q, R223A, K226E, L227S, and L240K) disrupt the chaperone activity of the Wind-ERp29 hybrid (10,11). We therefore asked whether these residues in ERp29 CTD might play a role in mediating PyV unfolding.…”