Itch/AIP4 mediates Deltex degradation through the formation of K29‐linked polyubiquitin chains
نویسندگان
چکیده
منابع مشابه
Itch/AIP4 mediates Deltex degradation through the formation of K29-linked polyubiquitin chains.
Deltex (DTX) and AIP4 are the human orthologues of the Drosophila deltex and Suppressor of deltex, which have been genetically described as being antagonistically involved in the Notch signalling pathway. Both genes encode E3 ubiquitin ligases of the RING (Really interesting new gene)-H2 and HECT (Homologous to E6AP carboxyl terminus) families, respectively. In an attempt to understand the mole...
متن کاملformation and evolution of regional organizations: the case study of the economic cooperation organization (eco)
abstract because of the many geopolitical, geo economical and geo strategically potentials and communicational capabilities of eco region, members can expand the convergence and the integration in base of this organization that have important impact on members development and expanding peace in international and regional level. based on quality analyzing of library findings and experts interv...
15 صفحه اولThe unexpected role of polyubiquitin chains in the formation of fibrillar aggregates
Ubiquitin is known to be one of the most soluble and stably folded intracellular proteins, but it is often found in inclusion bodies associated with various diseases including neurodegenerative disorders and cancer. To gain insight into this contradictory behaviour, we have examined the physicochemical properties of ubiquitin and its polymeric chains that lead to aggregate formation. We find th...
متن کاملProtein ubiquitination and formation of polyubiquitin chains without ATP, E1 and E2 enzymes.
Studying protein ubiquitination is difficult due to the complexity of the E1-E2-E3 ubiquitination cascade. Here we report the discovery that C-terminal ubiquitin thioesters can undergo direct transthiolation with the catalytic cysteine of the model HECT E3 ubiquitin ligase Rsp5 to form a catalytically active Rsp5∼ubiquitin thioester (Rsp5∼Ub). The resulting Rsp5∼Ub undergoes efficient autoubiqu...
متن کاملIn vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome.
Degradation of many eukaryotic proteins requires their prior ligation to polyubiquitin chains, which target substrates to the 26S proteasome, an abundant cellular protease. We describe a yeast deubiquitinating enzyme, Ubp14, that specifically disassembles unanchored ('free') ubiquitin chains in vitro, a specificity shared by mammalian isopeptidase T. Correspondingly, deletion of the UBP14 gene ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: EMBO reports
سال: 2006
ISSN: 1469-221X,1469-3178
DOI: 10.1038/sj.embor.7400822