Pathological mutations reveal the key role of the cytosolic iRhom2 N-terminus for phosphorylation-independent 14-3-3 interaction and ADAM17 binding, stability, and activity.
Katharina Bläsius, Lena Ludwig, Sarah Knapp, Charlotte Flasshove, Friederike Sonnabend, Diandra T. Keller, Nikola Tacken, Xintong Gao, Selcan Kahveci-Türköz, Caroline C. F. Grannemann, Aaron Babendreyer, Colin Adrain, Sebastian Huth, Jens Malte Baron, Andreas Ludwig, Stefan Düsterhöft
This study identifies a phosphorylation-independent 14-3-3 interaction site in iRhom2's N-terminus that regulates ADAM17 activity and shows how mutations in this region cause different pathological outcomes.
Cellular and Molecular Life Sciences · Feb 26, 2024Peer-reviewedMolecular Biology