Ontology highlight
ABSTRACT:
SUBMITTER: Wu X
PROVIDER: S-EPMC4147317 | biostudies-literature | 2014 Jun
REPOSITORIES: biostudies-literature
Wu Xiaomian X Fukushima Hidefumi H North Brian J BJ Nagaoka Yoshiyuki Y Nagashima Katsuyuki K Deng Feng F Okabe Koji K Inuzuka Hiroyuki H Wei Wenyi W
Oncotarget 20140601 12
CYLD negatively regulates the NF-κB signaling pathway and osteoclast differentiation largely through antagonizing TNF receptor-associated factor (TRAF)-mediated K63-linkage polyubiquitination in osteoclast precursor cells. CYLD activity is controlled by IκB kinase (IKK), but the molecular mechanism(s) governing CYLD protein stability remains largely undefined. Here, we report that SCFβ-TRCP regulates the ubiquitination and degradation of CYLD, a process dependent on prior phosphorylation of CYLD ...[more]