Proteomics

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E2 Rad6 controls cellular response to oxidative stress

ABSTRACT: Protein ubiquitination is an essential process that rapidly regulates protein synthesis, function, and fate in dynamic environments. Among its non-proteolytic functions, K63 ubiquitin accumulates in yeast cells exposed to oxidative stress, stalling ribosomes at elongation. K63 ubiquitin conjugates accumulate because of redox inhibition of the deubiquitinating enzyme Ubp2, however, the role and regulation of ubiquitin conjugating enzymes in this pathway remained unclear. Here we found that the E2 Rad6 binds and modifies elongating ribosomes during oxidative stress. We elucidated a mechanism by which Rad6 and its human homolog UBE2A are redox-regulated by forming reversible disulfides with the E1 activating enzyme, Uba1. We further showed that Rad6 activity is necessary to regulate translation, antioxidant defense, and adaptation to stress. Finally, we showed that Rad6 is required to induce phosphorylation of the translation initiation factor eIF2α, providing a novel link for K63 ubiquitin, elongation stalling, and the integrated stress response.

INSTRUMENT(S): Orbitrap Exploris 480

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

SUBMITTER: Gustavo Silva  

LAB HEAD: Gustavo Silva

PROVIDER: PXD025726 | Pride | 2022-08-12

REPOSITORIES: Pride

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Dataset's files

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Action DRS
SILAC1_Rad6_DTT.raw Raw
SILAC1_Rad6_Urea.raw Raw
SILAC2_Rad6_DTT.raw Raw
SILAC2_Rad6_Urea.raw Raw
evidence.txt Txt
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Publications

Redox-sensitive E2 Rad6 controls cellular response to oxidative stress via K63-linked ubiquitination of ribosomes.

Simões Vanessa V   Cizubu Blanche K BK   Harley Lana L   Zhou Ye Y   Pajak Joshua J   Snyder Nathan A NA   Bouvette Jonathan J   Borgnia Mario J MJ   Arya Gaurav G   Bartesaghi Alberto A   Silva Gustavo M GM  

Cell reports 20220501 8

Protein ubiquitination is an essential process that rapidly regulates protein synthesis, function, and fate in dynamic environments. Within its non-proteolytic functions, we showed that K63-linked polyubiquitinated conjugates heavily accumulate in yeast cells exposed to oxidative stress, stalling ribosomes at elongation. K63-ubiquitinated conjugates accumulate mostly because of redox inhibition of the deubiquitinating enzyme Ubp2; however, the role and regulation of ubiquitin-conjugating enzymes  ...[more]

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