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Energy sensor AMPK gamma regulates translation via phosphatase PPP6C independent of AMPK alpha

ABSTRACT: In this project, SILAC-based quantitative proteomics approach was applied for phosphoproteomics analysis. The light samples were treated with ddH2O as control group, and the medium samples labeled by 2D2 of lysine (K4) and 13C6 of arginine (R6) were treated with 2DG, while the heavy samples labeled by 13C615N2 of lysine (K8) and 13C615N4 of arginine (R10) were treated with 2DG in the presence of PPP6C knockdown. The peptides were analyzed by Orbitrap fusion instrument. Raw data was searched by MaxQuant software (version 1.6.6.0) against uniport human database.

ORGANISM(S): Homo Sapiens

SUBMITTER: Minjia Tan

PROVIDER: PXD038034 | iProX | Tue Nov 08 00:00:00 GMT 2022

REPOSITORIES: iProX

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Energy sensor AMPK gamma regulates translation via phosphatase PPP6C independent of AMPK alpha.

Zhou Qi Q Hao Bingbing B Cao Xiaolei X Gao Lin L Yu Zhenyue Z Zhao Yang Y Zhu Mingrui M Zhong Guoxuan G Chi Fangtao F Dai Xiaoming X Mao Jizhong J Zhu Yibing Y Rong Ping P Chen Liang L Bai Xueli X Ye Cunqi C Chen Shuai S Liang Tingbo T Li Li L Feng Xin-Hua XH Tan Minjia M Zhao Bin B

Molecular cell 20221115 24

Maintenance of energy level to drive movements and material exchange with the environment is a basic principle of life. AMP-activated protein kinase (AMPK) senses energy level and is a major regulator of cellular energy responses. The gamma subunit of AMPK senses elevated ratio of AMP to ATP and allosterically activates the alpha catalytic subunit to phosphorylate downstream effectors. Here, we report that knockout of AMPKγ, but not AMPKα, suppressed phosphorylation of eukaryotic translation elo ...[more]

PMID: 36384136

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