Proteomics

Dataset Information

0

Ubiquitylated-Rpn10 - Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism


ABSTRACT: MS/MS characterization of the proteasomal ubiquitin-receptor Rpn10 in its ubiquitylated state that together with structural and biochemical studies reveal a novel ubiquitin-binding patch on RPN10 that directs K84 ubiquitylation.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Oded Kleifeld  

LAB HEAD: Gali Prag

PROVIDER: PXD004761 | Pride | 2018-10-26

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
OK20130628_RPN10Mut_notcut.mzML Mzml
OK20130628_RPN10Mut_notcut.tandem Other
OK20130628_RPN10Mut_notcut.tandem.params Other
OK20130628_RPN10Mut_notcut.tandem.pep.xml Pepxml
OK20130628_RPN10WT_notcut.mzML Mzml
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Publications


Ubiquitin receptors decode ubiquitin signals into many cellular responses. Ubiquitin receptors also undergo coupled monoubiquitylation, and rapid deubiquitylation has hampered the characterization of the ubiquitylated state. Using bacteria that express a ubiquitylation apparatus, we purified and determined the crystal structure of the proteasomal ubiquitin-receptor Rpn10 in its ubiquitylated state. The structure shows a novel ubiquitin-binding patch that directs K84 ubiquitylation. Superimpositi  ...[more]

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