Proteomics

Dataset Information

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Identification of CTPS1 Filament Interacting Proteins


ABSTRACT: CTP synthase (CTPS) catalyzes the formation of CTP in de novo pyrimidine biosynthesis pathway. Compartmentalization of CTPS into filamentous structure is evolutionarily conserved from E.coli, yeast, Drosophila, mice to humans. Recently, we have demonstrated that histidine-mediated protein methylation promotes the formation of CTPS filament under glutamine and/or serum deprivation, which reduces its enzymatic activity and protects it from degradation. However, it is still unclear how the filament assembly takes place. In the current study, we used APEX2-mediated in vivo proximity labeling to identify proteins involved in CTPS filament formation.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Yu-Tsun Lin  

LAB HEAD: Jau-Song Yu

PROVIDER: PXD010921 | Pride | 2020-03-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20161104-CTP-APEX2-s01.raw Raw
20161104-CTP-APEX2-s02.raw Raw
20161104-CTP-APEX2-s03.raw Raw
20161104-CTP-APEX2-s04.raw Raw
20161104-CTP-APEX2-s05.raw Raw
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Publications


Under metabolic stress, cellular components can assemble into distinct membraneless organelles for adaptation. One such example is cytidine 5'-triphosphate synthase (CTPS, for which there are CTPS1 and CTPS2 forms in mammals), which forms filamentous structures under glutamine deprivation. We have previously demonstrated that histidine (His)-mediated methylation regulates the formation of CTPS filaments to suppress enzymatic activity and preserve the CTPS protein under glutamine deprivation, whi  ...[more]

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