Cargando…
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...
Autores principales: | Wauer, Tobias, Swatek, Kirby N, Wagstaff, Jane L, Gladkova, Christina, Pruneda, Jonathan N, Michel, Martin A, Gersch, Malte, Johnson, Christopher M, Freund, Stefan MV, Komander, David |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BlackWell Publishing Ltd
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4339119/ https://www.ncbi.nlm.nih.gov/pubmed/25527291 http://dx.doi.org/10.15252/embj.201489847 |
Ejemplares similares
-
An invisible ubiquitin conformation is required for efficient phosphorylation by PINK1
por: Gladkova, Christina, et al.
Publicado: (2017) -
Ubiquitin modifications
por: Swatek, Kirby N, et al.
Publicado: (2016) -
Assembly, analysis and architecture of atypical ubiquitin chains
por: Hospenthal, Manuela K., et al.
Publicado: (2013) -
Ubiquitin Linkage-Specific Affimers Reveal Insights into K6-Linked Ubiquitin Signaling
por: Michel, Martin A., et al.
Publicado: (2017) -
Assembly and Specific Recognition of K29- and K33-Linked Polyubiquitin
por: Michel, Martin A., et al.
Publicado: (2015)