IKK regulates the deubiquitinase CYLD at the postsynaptic density.

ABSTRACT: K63-linked polyubiquitination of proteins regulates their trafficking into specific cellular pathways such as endocytosis and autophagy. CYLD, a deubiquitinase specific for K63-linked polyubiquitins, is present in high quantities at the postsynaptic density (PSD). It was previously shown that, under excitatory conditions, CaMKII activates CYLD in a Ca(2+)-dependent manner. The observation that CYLD can also be phosphorylated in the absence of Ca(2+) in isolated PSDs led us to further explore the regulation of CYLD under basal conditions. A possible involvement of the autonomous form of CaMKII and IKK, both kinases known to be localized at the PSD, was examined. A CaMKII inhibitor CN21 had no effect on CYLD phosphorylation in the absence of Ca(2+), but two different IKK inhibitors, IKK16 an

SUBMITTER: Thein S 

PROVIDER: S-EPMC4126652 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature