Evidence map›Paper›PMID 28793258›Full record

ArticleCell reports2017

Crucial Roles for SIRT2 and AMPA Receptor Acetylation in Synaptic Plasticity and Memory.

Guan Wang, Shaomin Li, James Gilbert, Howard J Gritton, Zemin Wang, Zhangyuan Li, Xue Han, Dennis J Selkoe, Heng-Ye Man

Abstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
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

41 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Molecular Mechanisms of AMPA Receptor Trafficking in the Nervous System.International journal of molecular sciences · 2023
    Review
  10. Article
  11. SIRT2 Inhibition Rescues Neurodegenerative Pathology but Increases Systemic Inflammation in a Transgenic Mouse Model of Alzheimer's Disease.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2023
    Article
  12. The cardioprotective role of sirtuins is mediated in part by regulating KAmerican journal of physiology. Cell physiology · 2023
    Article
  13. Article
  14. iScience · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

9 authors.

Guan WangDepartment of Biology, Boston University, Boston, MA 02215, USA.
Shaomin LiCenter for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
James GilbertDepartment of Biology, Boston University, Boston, MA 02215, USA.
Howard J GrittonDepartment of Biomedical Engineering, Boston University, Boston, MA 02215, USA.
Zemin WangCenter for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Zhangyuan LiCenter for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Xue HanDepartment of Biomedical Engineering, Boston University, Boston, MA 02215, USA.
Dennis J SelkoeCenter for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Heng-Ye ManDepartment of Biology, Boston University, Boston, MA 02215, USA; Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA 02118, USA. Electronic address: hman@bu.edu.

Funding

Molecular Mechanisms of Homeostatic Synaptic PlasticityR01MH079407 · NIMH · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MAN, HENGYE · 2008 to 2018
$3.9M
NIMH NIH HHS R01 MH079407
6 · The paper itself

Abstract

AMPA receptors (AMPARs) mediate fast excitatory synaptic transmission and are crucial for synaptic plasticity, learning, and memory. However, the molecular control of AMPAR stability and its neurophysiological significance remain unclear. Here, we report that AMPARs are subject to lysine acetylation at their C termini. Acetylation reduces AMPAR internalization and degradation, leading to increased cell-surface localization and prolonged receptor half-life. Through competition for the same lysine residues, acetylation intensity is inversely related to the levels of AMPAR ubiquitination. We find that sirtuin 2 (SIRT2) acts as an AMPAR deacetylase regulating AMPAR trafficking and proteostasis. SIRT2 knockout mice (Sirt2

Indexed as

MemoryNeuronal PlasticityProtein Processing, Post-TranslationalAcetylationAnimalsCells, CulturedFemaleHEK293 CellsHumansMaleMiceMice, Inbred C57BLNeuronsProtein TransportProteolysisRatsReceptors, AMPASirt2 protein, ratSirtuin 2acetylationAMPA receptorsAMPARscognitive functiondeacetylaselearning and memoryreceptor traffickingsirtuin 2synaptic plasticityubiquitination

Identifiers

PMID28793258
PMCPMC5584878

What OpenQuestion holds

Textmetadata
LicenceTDM
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.