Evidence map›Paper›PMID 30366365›Full record

ReviewInternational journal of molecular sciences2018

Reciprocal Regulation of AMPK/SNF1 and Protein Acetylation.

Ales Vancura, Shreya Nagar, Pritpal Kaur, Pengli Bu, Madhura Bhagwat, Ivana Vancurova

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.

  1. Pooled it
  2. Toward Complex Polyketide Biosynthesis inJournal of microbiology and biotechnology · 2026
    Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Frontiers in cellular and infection microbiology · 2025
    Article
  13. Astragalin fromAntioxidants (Basel, Switzerland) · 2024
    Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Sirtuin family in autoimmune diseases.Frontiers in immunology · 2023
    Review
  20. The sirtuin family in health and disease.Signal transduction and targeted therapy · 2022
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Ales VancuraDepartment of Biological Sciences, St. John's University, New York, NY 11439, USA. vancuraa@stjohns.edu.
Shreya NagarDepartment of Biological Sciences, St. John's University, New York, NY 11439, USA. shreya.nagar17@my.stjohns.edu.
Pritpal KaurDepartment of Biological Sciences, St. John's University, New York, NY 11439, USA. pritpal.kaur17@my.stjohns.edu.
Pengli BuDepartment of Biological Sciences, St. John's University, New York, NY 11439, USA. bup@stjohns.edu.
Madhura BhagwatDepartment of Biological Sciences, St. John's University, New York, NY 11439, USA. madhura.bhagwat16@my.stjohns.edu.
Ivana VancurovaDepartment of Biological Sciences, St. John's University, New York, NY 11439, USA. vancuroi@stjohns.edu.ORCID 0000-0002-7508-7396
St. John's University · US

Funding

Transcriptional Regulation and MetabolismR15GM120710 · NIGMS · ST. JOHN'S UNIVERSITY · PI VANCURA, ALES · 2016 to 2016
$495k
National Institutes of Health GM120710NIGMS NIH HHS R15 GM120710
6 · The paper itself

Abstract

Adenosine monophosphate (AMP)-activated protein kinase (AMPK) serves as an energy sensor and master regulator of metabolism. In general, AMPK inhibits anabolism to minimize energy consumption and activates catabolism to increase ATP production. One of the mechanisms employed by AMPK to regulate metabolism is protein acetylation. AMPK regulates protein acetylation by at least five distinct mechanisms. First, AMPK phosphorylates and inhibits acetyl-CoA carboxylase (ACC) and thus regulates acetyl-CoA homeostasis. Since acetyl-CoA is a substrate for all lysine acetyltransferases (KATs), AMPK affects the activity of KATs by regulating the cellular level of acetyl-CoA. Second, AMPK activates histone deacetylases (HDACs) sirtuins by increasing the cellular concentration of NAD⁺, a cofactor of sirtuins. Third, AMPK inhibits class I and II HDACs by upregulating hepatic synthesis of α-hydroxybutyrate, a natural inhibitor of HDACs. Fourth, AMPK induces translocation of HDACs 4 and 5 from the nucleus to the cytoplasm and thus increases histone acetylation in the nucleus. Fifth, AMPK directly phosphorylates and downregulates p300 KAT. On the other hand, protein acetylation regulates AMPK activity. Sirtuin SIRT1-mediated deacetylation of liver kinase B1 (LKB1), an upstream kinase of AMPK, activates LKB1 and AMPK. AMPK phosphorylates and inactivates ACC, thus increasing acetyl-CoA level and promoting LKB1 acetylation and inhibition. In yeast cells, acetylation of Sip2p, one of the regulatory β-subunits of the SNF1 complex, results in inhibition of SNF1. This results in activation of ACC and reduced cellular level of acetyl-CoA, which promotes deacetylation of Sip2p and activation of SNF1. Thus, in both yeast and mammalian cells, AMPK/SNF1 regulate protein acetylation and are themselves regulated by protein acetylation.

Indexed as

AcetylationAcetyl Coenzyme AAMP-Activated Protein KinasesAnimalsEpigenomicsHistone DeacetylasesHumansProtein Serine-Threonine KinasesAcetyl Coenzyme AAMP-Activated Protein KinasesHistone DeacetylasesProtein Serine-Threonine KinasesSNF1-related protein kinasesacetyl-CoAAMP-activated protein kinaseepigeneticsHDACsKATsNAD+protein acetylation

Identifiers

PMID30366365
PMCPMC6274705
OpenAlexW2898531532

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.