Proteomics

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CTLH E3 Ligase Regulates the Degradation of HMG-CoA Synthase 1 Through the Pro/N-end Rule Pathway


ABSTRACT: Supporting raw MS data for paper (doi: 10.1016/j.molcel.2024.04.026) by Yi S.A. et al, titled "CTLH E3 Ligase Regulates the Degradation of HMG-CoA Synthase 1 Through the Pro/N-end Rule Pathway". Index of RAW files uploaded: - Related to Supplementary Table 1 (HA-9-81-X | WT (1), ATG7KO (2), RB1CC1 (3): whole proteome (Unimod: 35; 2016; 4)). - Related to Supplementary Table 2 - Proteome (HA-1-50: whole proteome (Unimod: 35; 2016; 4)). - Related to Supplementary Table 2 - PhosphoSites (HA-1-50_Phos: phospho proteome (Unimod: 35; 21; 2016; 4)) - Related to Supplementary Table 3 (Yis-1-49: whole proteome (Unimod: 35; 2016; 4))

INSTRUMENT(S): Orbitrap Eclipse

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

SUBMITTER: Heeseon An   Alban Ordureau  

PROVIDER: MSV000090814 | MassIVE | Tue Nov 29 20:21:00 GMT 2022

REPOSITORIES: MassIVE

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Publications

mTORC1-CTLH E3 ligase regulates the degradation of HMG-CoA synthase 1 through the Pro/N-degron pathway.

Yi Sang Ah SA   Sepic Sara S   Schulman Brenda A BA   Ordureau Alban A   An Heeseon H  

Molecular cell 20240523 11


Mammalian target of rapamycin (mTOR) senses changes in nutrient status and stimulates the autophagic process to recycle amino acids. However, the impact of nutrient stress on protein degradation beyond autophagic turnover is incompletely understood. We report that several metabolic enzymes are proteasomal targets regulated by mTOR activity based on comparative proteome degradation analysis. In particular, 3-hydroxy-3-methylglutaryl (HMG)-coenzyme A (CoA) synthase 1 (HMGCS1), the initial enzyme i  ...[more]

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