The Tumour Suppressor TMEM127 Is a Nedd4-Family E3 Ligase Adaptor Required by Salmonella SteD to Ubiquitinate and Degrade MHC Class II Molecules
Eric Alix, Camilla Godlee, Ondřej Černý, Samkeliso Blundell, Romina Tocci, Sophie A. Matthews, Mei Liu, Jonathan N. Pruneda, Kirby N. Swatek, David Komander, Tabitha Sleap, David W. Holden
Abstract
T cell activation. We found that TMEM127 contains a canonical PPxY motif, which was required for binding to WWP2. SteD bound to TMEM127 and enabled TMEM127 to interact with and induce ubiquitination of mature MHCII. Furthermore, SteD also underwent TMEM127- and WWP2-dependent ubiquitination, which both contributed to its degradation and augmented its activity on mMHCII.
Topics & Concepts
Ubiquitin ligaseBiologyNEDD4Cell biologyMHC class ISuppressorSignal transducing adaptor proteinUbiquitinMHC class IIMajor histocompatibility complexGeneticsCancerAntigenSignal transductionGeneUbiquitin and proteasome pathwaysAutophagy in Disease and TherapyCancer Research and Treatments