NEDD8 S65 phosphorylation under different stress conditions
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive HF
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: 
Katrin Stuber
LAB HEAD: Prof. Dr. Martin Scheffner
PROVIDER: PXD027477 | Pride | 2021-11-03
REPOSITORIES: Pride
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Project description:In this project we present for the first time a proteome-wide interaction study of S65 phosphorylated NEDD8 and ubiquitin (Ub). By using cell extracts and affinity enrichment coupled to mass spectrometry, we show that pNEDD8 and pUb have different interactomes that are also distinct from those of the non-modified forms. Among the preferential pNEDD8 interactors are HSP70 family members and, indeed, pNEDD8 stimulates HSP70 ATPase activity more pronouncedly than non-modified NEDD8. Our findings provide evidence that phosphorylation of Ub and NEDD8 at S65 is involved in stress response signaling and underscore the importance of studying non-covalent interactions of NEDD8 in particular and post-translational modifications of Ubls in general.
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Project description:Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be phosphorylated. However, the effect of this modification on ubiquitin function is largely unknown. Here, we performed in vivo and in vitro characterization of the effects of phosphorylation of yeast ubiquitin at position serine 65. We find ubiquitin S65 phosphorylation to be regulated under oxidative stress, occurring in tandem with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, and substrate targeting. These results demonstrate that phosphorylation represents an additional mode of ubiquitin regulation with broad implications in cellular physiology.
2015-07-07 | PXD002201 | Pride
Project description:Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be phosphorylated. However, the effect of this modification on ubiquitin function is largely unknown. Here, we performed in vivo and in vitro characterization of the effects of phosphorylation of yeast ubiquitin at position serine 65. We find ubiquitin S65 phosphorylation to be regulated under oxidative stress, occurring in tandem with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, and substrate targeting. These results demonstrate that phosphorylation represents an additional mode of ubiquitin regulation with broad implications in cellular physiology.
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Project description:Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be phosphorylated. However, the effect of this modification on ubiquitin function is largely unknown. Here, we performed in vivo and in vitro characterization of the effects of phosphorylation of yeast ubiquitin at position serine 65. We find ubiquitin S65 phosphorylation to be regulated under oxidative stress, occurring in tandem with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, and substrate targeting. These results demonstrate that phosphorylation represents an additional mode of ubiquitin regulation with broad implications in cellular physiology.
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Project description:Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be phosphorylated. However, the effect of this modification on ubiquitin function is largely unknown. Here, we performed in vivo and in vitro characterization of the effects of phosphorylation of yeast ubiquitin at position serine 65. We find ubiquitin S65 phosphorylation to be regulated under oxidative stress, occurring in tandem with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, and substrate targeting. These results demonstrate that phosphorylation represents an additional mode of ubiquitin regulation with broad implications in cellular physiology.
2015-07-07 | PXD002199 | Pride
Project description:Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be phosphorylated. However, the effect of this modification on ubiquitin function is largely unknown. Here, we performed in vivo and in vitro characterization of the effects of phosphorylation of yeast ubiquitin at position serine 65. We find ubiquitin S65 phosphorylation to be regulated under oxidative stress, occurring in tandem with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, and substrate targeting. These results demonstrate that phosphorylation represents an additional mode of ubiquitin regulation with broad implications in cellular physiology.
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Project description:Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be phosphorylated. However, the effect of this modification on ubiquitin function is largely unknown. Here, we performed in vivo and in vitro characterization of the effects of phosphorylation of yeast ubiquitin at position serine 65. We find ubiquitin S65 phosphorylation to be regulated under oxidative stress, occurring in tandem with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, and substrate targeting. These results demonstrate that phosphorylation represents an additional mode of ubiquitin regulation with broad implications in cellular physiology.
2015-07-07 | PXD002197 | Pride
Project description:Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be phosphorylated. However, the effect of this modification on ubiquitin function is largely unknown. Here, we performed in vivo and in vitro characterization of the effects of phosphorylation of yeast ubiquitin at position serine 65. We find ubiquitin S65 phosphorylation to be regulated under oxidative stress, occurring in tandem with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, and substrate targeting. These results demonstrate that phosphorylation represents an additional mode of ubiquitin regulation with broad implications in cellular physiology.
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Project description:Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be phosphorylated. However, the effect of this modification on ubiquitin function is largely unknown. Here, we performed in vivo and in vitro characterization of the effects of phosphorylation of yeast ubiquitin at position serine 65. We find ubiquitin S65 phosphorylation to be regulated under oxidative stress, occurring in tandem with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, and substrate targeting. These results demonstrate that phosphorylation represents an additional mode of ubiquitin regulation with broad implications in cellular physiology.
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