Evidence map›Paper›PMID 20685962›Full record

ArticleMolecular biology of the cell2010

Identification of a nuclear export signal in the catalytic subunit of AMP-activated protein kinase.

Nevzat Kazgan, Tyisha Williams, Lawrence J Forsberg, Jay E Brenman

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

68 citing papers in PubMed, 120 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Spatial regulation of AMPK activity under oxidative stress requires LKB1.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. New insights into activation and function of the AMPK.Nature reviews. Molecular cell biology · 2023
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. AMPK Localization: A Key to Differential Energy Regulation.International journal of molecular sciences · 2021
    Review
  20. Review

8 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Nevzat KazganNeuroscience Center, University of North Carolina Chapel Hill School of Medicine, Chapel Hill, NC 27599-7250, USA.
Tyisha Williams
Lawrence J Forsberg
Jay E Brenman
Center for Neurosciences · USUniversity of North Carolina at Chapel Hill · US

Funding

Genetic Analysis of Dendrite and Dendritic Filopodia FormationR01MH073155 · NIMH · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BRENMAN, JAY · 2006 to 2010
$1.6M
Genetic Elucidation of AMP-Activated Protein Kinase Signaling MechanismsR01NS080108 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BRENMAN, JAY · 2012 to 2016
$1.6M
NIMH NIH HHS MH073155NIMH NIH HHS R01 MH073155NINDS NIH HHS R01 NS080108
6 · The paper itself

Abstract

The metabolic regulator AMP-activated protein kinase (AMPK) maintains cellular homeostasis through regulation of proteins involved in energy-producing and -consuming pathways. Although AMPK phosphorylation targets include cytoplasmic and nuclear proteins, the precise mechanisms that regulate AMPK localization, and thus its access to these substrates, are unclear. We identify highly conserved carboxy-terminal hydrophobic amino acids that function as a leptomycin B-sensitive, CRM1-dependent nuclear export sequence (NES) in the AMPK catalytic subunit (AMPKα). When this sequence is modified AMPKα shows increased nuclear localization via a Ran-dependent import pathway. Cytoplasmic localization can be restored by substituting well-defined snurportin-1 or protein kinase A inhibitor (PKIA) CRM1-binding NESs into AMPKα. We demonstrate a functional requirement in vivo for the AMPKα carboxy-terminal NES, as transgenic Drosophila expressing AMPKα lacking this NES fail to rescue lethality of AMPKα null mutant flies and show decreased activation loop phosphorylation under heat-shock stress. Sequestered to the nucleus, this truncated protein shows highly reduced phosphorylation at the key Thr172 activation residue, suggesting that AMPK activation predominantly occurs in the cytoplasm under unstressed conditions. Thus, modulation of CRM1-mediated export of AMPKα via its C-terminal NES provides an additional mechanism for cells to use in the regulation of AMPK activity and localization.

Indexed as

Catalytic DomainNuclear Export SignalsAmino AcidsAmino Acid SequenceAMP-Activated Protein KinasesAnimalsCell LineCell NucleusCytoplasmDrosophila melanogasterEnzyme ActivationHeat-Shock ResponseHumansIsoenzymesMiceMolecular Sequence DataAmino AcidsAMP-Activated Protein KinasesIsoenzymesMutant ProteinsNuclear Export SignalsProtein Subunitsran GTP-Binding Protein

Identifiers

PMID20685962
PMCPMC2947478
OpenAlexW2165985172

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.