Contribution of lysine 11-linked ubiquitination to MIR2-mediated major histocompatibility complex class I internalization.

ABSTRACT: The polyubiquitin chain is generated by the sequential addition of ubiquitin moieties to target molecules, a reaction between specific lysine residues that is catalyzed by E3 ubiquitin ligase. The Lys(48)-linked and Lys(63)-linked polyubiquitin chains are well established inducers of proteasome-dependent degradation and signal transduction, respectively. The concept has recently emerged that polyubiquitin chain-mediated regulation is even more complex because various types of atypical polyubiquitin chains have been discovered in vivo. Here, we demonstrate that a novel complex ubiquitin chain functions as an internalization signal for major histocompatibility complex class I (MHC I) membrane proteins in vivo. Using a tetracycline-inducible expression system and quantitative mass spectrometr

SUBMITTER: Goto E 

PROVIDER: S-EPMC2975155 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature