Proteomics

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Global Phosphoproteomic Analysis Reveals ARMC10 as an AMPK Substrate that Regulates Mitochondrial Dynamics


ABSTRACT: AMP-activated protein kinase (AMPK) is a key regulator of cellular energy homeostasis. Although AMPK has been studied extensively in cellular processes, understanding of its substrates and downstream functional network, and their contributions to cell fate and disease development, remains incomplete. To elucidate the AMPK-dependent signaling pathways, we performed global quantitative phosphoproteomic analysis using wild-type and AMPK1/2-double knockout cells and discovered 160 AMPK-dependent phosphorylation sites.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Zhen Chen  

LAB HEAD: Junjie Chen

PROVIDER: PXD011696 | Pride | 2019-01-16

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
13204_E_Zhen_Pho_KO_02_H_01.raw Raw
13204_E_Zhen_Pho_KO_02_H_02.raw Raw
13204_E_Zhen_Pho_KO_02_H_03.raw Raw
13204_E_Zhen_Pho_KO_02_H_04.raw Raw
13204_E_Zhen_Pho_KO_02_H_05.raw Raw
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Publications

Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics.

Chen Zhen Z   Lei Caoqi C   Wang Chao C   Li Nan N   Srivastava Mrinal M   Tang Mengfan M   Zhang Huimin H   Choi Jong Min JM   Jung Sung Yun SY   Qin Jun J   Chen Junjie J  

Nature communications 20190110 1


AMP-activated protein kinase (AMPK) is a key regulator of cellular energy homeostasis. Although AMPK has been studied extensively in cellular processes, understanding of its substrates and downstream functional network, and their contributions to cell fate and disease development, remains incomplete. To elucidate the AMPK-dependent signaling pathways, we performed global quantitative phosphoproteomic analysis using wild-type and AMPKα1/α2-double knockout cells and discovered 160 AMPK-dependent p  ...[more]

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