Novel interaction of the co-chaperone DNAJC12 with phenylalanine hydroxylase variants
Researchers from the lab of Aurora Martinez describe a novel mechanism for the degradation of enzymes involved in phenylketonuria and other neurometabolic disorders.
Hovedinnhold
We showed that mutant phenylalanine hydroxylase (PAH) exhibits increased ubiquitination compared with normal PAH. We also showed that the co-chaperone DNAJC12 interacts with monoubiquitin-tagged PAH. The results indicate a role of DNAJC12 in the processing of misfolded ubiquitinated PAH.
Our image was featured on the cover of the April 2019 issue of Human Mutation.
Original article
"Phenylalanine hydroxylase variants interact with the co‐chaperone DNAJC12"
Authors: Kunwar Jung‐KC, Nastassja Himmelreich, Karina S. Prestegård, Tie‐Jun Sten Shi, Tanja Scherer, Ming Ying, Ana Jorge‐Finnigan, Beat Thöny, Nenad Blau, Aurora Martinez
Human Mutation, 22 January 2019
