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Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis
The protein kinase PINK1 was recently shown to phosphorylate ubiquitin (Ub) on Ser65, and phosphoUb activates the E3 ligase Parkin allosterically. Here, we show that PINK1 can phosphorylate every Ub in Ub chains. Moreover, Ser65 phosphorylation alters Ub structure, generating two conformations in so...
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| Published in: | EMBO J |
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| Main Authors: | , , , , , , , , , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
BlackWell Publishing Ltd
2015
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4339119/ https://ncbi.nlm.nih.gov/pubmed/25527291 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.15252/embj.201489847 |
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