Proteomics

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Protein abundance changes and ubiquitylation targets identified upon inhibition of the proteasome with Syringolin A

ABSTRACT: The numerous roles of the ubiquitin proteasome system (UPS) in cellular control have triggered interest in the identification of these ubiquitylation targets and their sites of ubiquitylation. For the identification of ubiquitylated proteins we employed affinity enrichment using an ubiquitin binding domains (UBAs). A change in the experimental set-up allowed for the identification of proteins that so far have been refractory to identification. We also investigated the changes in protein abundance upon interfering with the UPS by inhibition of the proteasome with the specific inhibitor Syringolin A and using a mutant overexpressing ubiquitin that cannot form K48-linked polyubiquitin chains.

INSTRUMENT(S): LTQ Orbitrap XL

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Katja Baerenfaller  

LAB HEAD: Katja Baerenfaller

PROVIDER: PXD000567 | Pride | 2014-04-15

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
20110321_03_sylA_1_ED.RAW Raw
20110321_03_sylA_1_ED.mgf Mgf
20110321_04_sylA_2_ED.RAW Raw
20110321_04_sylA_2_ED.mgf Mgf
20110321_05_sylA_3_ED.RAW Raw
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Protein abundance changes and ubiquitylation targets identified after inhibition of the proteasome with syringolin A.

Svozil Julia J   Hirsch-Hoffmann Matthias M   Dudler Robert R   Gruissem Wilhelm W   Baerenfaller Katja K  

Molecular & cellular proteomics : MCP 20140413 6

As proteins are the main effectors inside cells, their levels need to be tightly regulated. This is partly achieved by specific protein degradation via the Ubiquitin-26S proteasome system (UPS). In plants, an exceptionally high number of proteins are involved in Ubiquitin-26S proteasome system-mediated protein degradation and it is known to regulate most, if not all, important cellular processes. Here, we investigated the response to the inhibition of the proteasome at the protein level treating  ...[more]

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