Proteomics

Dataset Information

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G6PD K403 acetylation-dependent PTM

ABSTRACT: To identify acetylation-dependent posttranslational modifications (PTMs) of G6PD, site-specifically acetylated and Flag-tagged G6PD was expressed in HEK293T cells by genetically encoding the incorporation of acetylated lysine in response to an in-frame TAG stop codon. K403-acetylated G6PD (sample) and K414-acetylated G6PD (control) were co-expressed with WT Fyn kinase and a catalytically inactive mutant of Fyn (FynDN). G6PD was immunoprecipitated using anti-Flag beads before MS analysis.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Eyal Arbely  

LAB HEAD: Eyal Arbely

PROVIDER: PXD041775 | Pride | 2023-10-24

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
Seq72977_QE3-modifications.msf Msf
Seq72977_QE3_pWT-Fyn.raw Raw
Seq72978_QE3-modifications.msf Msf
Seq72978_QE3_pWT-FynDN.raw Raw
Seq72979_QE3-modifications.msf Msf
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Publications

Acetylation-dependent coupling between G6PD activity and apoptotic signaling.

Wu Fang F   Muskat Natali H NH   Dvilansky Inbar I   Koren Omri O   Shahar Anat A   Gazit Roi R   Elia Natalie N   Arbely Eyal E  

Nature communications 20231005 1

Lysine acetylation has been discovered in thousands of non-histone human proteins, including most metabolic enzymes. Deciphering the functions of acetylation is key to understanding how metabolic cues mediate metabolic enzyme regulation and cellular signaling. Glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme in the pentose phosphate pathway, is acetylated on multiple lysine residues. Using site-specifically acetylated G6PD, we show that acetylation can activate (AcK89) and inhi  ...[more]

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