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cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
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Updated: May 21, 2026

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Published on: May 16, 2021

Metformin interacts with AMPK through binding to γ subunit.

Yaya Zhang1, Yongjun Wang, Chuanen Bao

  • 1Department of Oncology, The 174th Hospital of the Chinese People's Liberation Army, The Affiliated Chenggong Hospital of Xiamen University, Xiamen 361003, Fujian, People's Republic of China.

Molecular and Cellular Biochemistry
|May 31, 2012
PubMed
Summary
This summary is machine-generated.

Metformin activates 5'-adenosine monophosphate-activated protein kinase (AMPK) by binding to its gamma subunit. This interaction influences energy regulation, suggesting a direct molecular mechanism for metformin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Metformin is an energy regulator that activates 5'-adenosine monophosphate-activated protein kinase (AMPK).
  • The precise molecular target of metformin within AMPK remains uncertain.
  • AMPK is crucial for maintaining cellular energy homeostasis.

Purpose of the Study:

  • To investigate the direct interaction between metformin and AMPK.
  • To identify the specific subunit of AMPK that metformin binds to.
  • To elucidate the molecular mechanism of metformin's action on AMPK.

Main Methods:

  • Western blot analysis to confirm metformin's effect on AMPK and ACC.
  • Molecular docking to predict metformin's binding site on AMPK.
  • Fluorescence spectroscopy and ForteBio assays to assess binding affinity.
  • Circular dichroism (CD) spectroscopy to analyze conformational changes upon binding.

Main Results:

  • Metformin promotes AMPK activation and ACC inactivation in HepG2 cells.
  • Molecular docking suggests metformin interacts with the gamma (γ) subunit of AMPK.
  • Binding assays show higher affinity of metformin to the γ-AMPK subunit compared to the alpha (α) subunit.
  • CD spectra reveal metformin binding to γ-AMPK decreases alpha-helicity, with minimal effect on α-AMPK.

Conclusions:

  • Metformin directly interacts with the gamma subunit of AMPK.
  • This interaction is likely the mechanism by which metformin modulates AMPK activity.
  • The findings provide a molecular basis for metformin's role in energy regulation.