A co-opted ISG15-USP18 binding mechanism normally reserved for deISGylation controls type I IFN signalling
A. Vasou, K. Nightingale, V. Cetkovska, J. Scheler, C. G. Bamford, J. Andrejeva, U. Schwarz-Linek, R. E. Randall, J. McLauchlan, M. P. Weekes, D. Bogunovic, D. J. Hughes
The paper identifies a new function of ISG15 in stabilizing USP18 through non-covalent interactions, revealing a mechanism that controls type I IFN signalling.
bioRxiv · Jun 1, 2021 · PreprintImmunology