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NEDDylation promotes nuclear protein aggregation and protects the Ubiquitin Proteasome System upon proteotoxic stress

ABSTRACT: SILAC quantitative mass spectrometry analysis on protein aggregates induced upon heat shock. Two separate performed analysis: A) control siRNA cells (light) with siRNA NEDD8 cells (heavy) and B) control cells (light) with MLN4924 treated cells (heavy). In all conditions cells were heat shocked at 43oC before cell mixing and aggregate isolation. Samples were solubilised in 2xSDS Laemmli buffer, 50ug of protein were run for 15min on 4-12% precast NuPAGE and coomassie blue stained. Lanes were cut in 2 gel pieces before in gel trypsin digestion and mass spectrometry analysis.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Dimitris Xirodimas

PROVIDER: MSV000082623 | MassIVE | Tue Jul 17 07:23:00 BST 2018

REPOSITORIES: MassIVE

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NEDDylation promotes nuclear protein aggregation and protects the Ubiquitin Proteasome System upon proteotoxic stress.

Maghames Chantal M CM Lobato-Gil Sofia S Perrin Aurelien A Trauchessec Helene H Rodriguez Manuel S MS Urbach Serge S Marin Philippe P Xirodimas Dimitris P DP

Nature communications 20181022 1

Spatial management of stress-induced protein aggregation is an integral part of the proteostasis network. Protein modification by the ubiquitin-like molecule NEDD8 increases upon proteotoxic stress and it is characterised by the formation of hybrid NEDD8/ubiquitin conjugates. However, the biological significance of this response is unclear. Combination of quantitative proteomics with biological analysis shows that, during proteotoxic stress, NEDDylation promotes nuclear protein aggregation, incl ...[more]

PMID: 30349034

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