Axotrophin a RING-variant domain protein acts as E3-ubiquitin-ligase and ubiquitinates the microtubule-associated protein tau
| Autor: | Katharina Flach, Max Holzer, Ellen Ramminger, Thomas Arendt, Franziska Albrecht |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
chemistry.chemical_classification
biology General Neuroscience lcsh:QP351-495 Protein domain Tau protein Protein aggregation Protein ubiquitination lcsh:RC321-571 Ubiquitin ligase Cell biology Cellular and Molecular Neuroscience lcsh:Neurophysiology and neuropsychology Enzyme Biochemistry Microtubule associated protein tau Ubiquitin chemistry biology.protein lcsh:Neurosciences. Biological psychiatry. Neuropsychiatry |
| Zdroj: | BMC Neuroscience, Vol 8, Iss Suppl 1, p P15 (2007) |
| ISSN: | 1471-2202 |
| DOI: | 10.1186/1471-2202-8-s1-p15 |
| Popis: | Axotrophin harbours a C4HC3 zinc-finger-like motif in the C-terminus, which is referred to as Ring-variant domain and has been implicated in protein ubiquitination. Recombinant expression and refolding of the C-terminus of axotrophin allowed us to test the E3-ubiquitinligase activity. We found that axotrophin shows E3-ubiquitin-ligase activity in combination with several E2 enzymes and becomes autoubiquitinated. Ubiquitination of tau protein but not KLC1, another axotrophin-interacting protein, was mediated by axotrophin. Further investigation of ubiquitination effects on the protein tau will give more insights about the E3-ubiquitinligase axotrophin and especially its role in AD. from Annual Meeting of the Study Group Neurochemistry. International Conference of the Gesellschaft fur Biochemie und Molekularbiologie 2006 (GBM 2006): Molecular pathways in health and disease of the nervous system Witten, Germany. 28–30 September 2006 |
| Databáze: | OpenAIRE |
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