ArticleMolecular & cellular proteomics : MCP2020
AMPK Interactome Reveals New Function in Non-homologous End Joining DNA Repair.
Article in Molecular & cellular proteomics : MCP, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Expanding Synthetic Lethality in DNA Damage Response-Defective Cancers Through Stress Phenotype-Guided Kinase Targeting.International journal of molecular sciences · 2026Review
- Mitochondrial dysfunction in oocytes: implications for fertility and ageing.Journal of ovarian research · 2025Review
- Proteomic analysis of ferroptosis pathways reveals a role of CEPT1 in suppressing ferroptosis.Protein & cell · 2024Article
- AMP-activated protein kinase - a journey from 1 to 100 downstream targets.The Biochemical journal · 2022Article
- USP7 substrates identified by proteomics analysis reveal the specificity of USP7.Genes & development · 2022Article
- AMPK: restoring metabolic homeostasis over space and time.Molecular cell · 2021Review
- Mass spectrometry-based protein‒protein interaction techniques and their applications in studies of DNA damage repair.Journal of Zhejiang University. Science. B · 2021Review
- Roles of AMP-Activated Protein Kinase (AMPK) in Mammalian Reproduction.Frontiers in cell and developmental biology · 2020Review
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
Adenosine monophosphate-activated protein kinase (AMPK) is an obligate heterotrimer that consists of a catalytic subunit (α) and two regulatory subunits (β and γ). AMPK is a key enzyme in the regulation of cellular energy homeostasis. It has been well studied and is known to function in many cellular pathways. However, the interactome of AMPK has not yet been systematically established, although protein-protein interaction is critically important for protein function and regulation. Here, we used tandem-affinity purification, coupled with mass spectrometry (TAP-MS) analysis, to determine the interactome of AMPK and its functions. We conducted a TAP-MS analysis of all seven AMPK subunits. We identified 138 candidate high-confidence interacting proteins (HCIPs) of AMPK, which allowed us to build an interaction network of AMPK complexes. Five candidate AMPK-binding proteins were experimentally validated, underlining the reliability of our data set. Furthermore, we demonstrated that AMPK acts with a strong AMPK-binding protein, Artemis, in non-homologous end joining. Collectively, our study established the first AMPK interactome and uncovered a new function of AMPK in DNA repair.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.