Evidence map›Paper›PMID 26945062›Full record

ArticleThe Journal of biological chemistry2016

Capillary Isoelectric Focusing of Akt Isoforms Identifies Highly Dynamic Phosphorylation in Neuronal Cells and Brain Tissue.

Sandra Schrötter, George Leondaritis, Britta J Eickholt

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Role of Akt isoforms in neuronal insulin signaling and resistance.Cellular and molecular life sciences : CMLS · 2021
    Article
  8. Article
  9. Article
  10. Akt3 Regulates the Tissue-Specific Response to Copaiba Essential Oil.International journal of molecular sciences · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

Sandra SchrötterFrom the Charité-Universitätsmedizin Berlin, Cluster of Excellence NeuroCure and Institute of Biochemistry, Berlin 10117, Germany.
George LeondaritisFrom the Charité-Universitätsmedizin Berlin, Cluster of Excellence NeuroCure and Institute of Biochemistry, Berlin 10117, Germany.
Britta J EickholtFrom the Charité-Universitätsmedizin Berlin, Cluster of Excellence NeuroCure and Institute of Biochemistry, Berlin 10117, Germany Britta.Eickholt@charite.de.
Charité - Universitätsmedizin Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PI3K/PTEN/Akt pathway has been established as a core signaling pathway that is crucial for the integration of neurons into neuronal circuits and the maintenance of the architecture and function of neurons in the adult brain. Akt1-3 kinases are specifically activated by two phosphorylation events on residues Thr(308) and Ser(473) upon growth factor signaling, which subsequently phosphorylate a vast cohort of downstream targets. However, we still lack a clear understanding of the complexity and regulation of isoform specificity within the PI3K/PTEN/Akt pathway. We utilized a capillary-based isoelectric focusing method to study dynamics of Akt phosphorylation in neuronal cells and the developing brain and identify previously undescribed features of Akt phosphorylation and activation. First, we show that the accumulation of multiple phosphorylation events on Akt forms occur concurrently with Ser(473) and Thr(308) phosphorylation upon acute PI3K activation and provide evidence for uncoupling of Ser(473) and Thr(308) phosphorylation, as well as differential sensitivities of Akt1 forms upon PI3K inhibition. Second, we detect a transient shift in Akt isoform phosphorylation and activation pattern during early postnatal brain development, at stages corresponding to synapse development and maturation. Third, we show differential sensitivities of Ser(473)-Akt species to PTEN deletion in mature neurons, which suggests inherent differences in the Akt pools that are accessible to growth factors as compared with the pools that are controlled by PTEN. Our study demonstrates the presence of complex phosphorylation events of Akt in a time- and signal-dependent manner in neurons.

Indexed as

AdultAnimalsBlotting, WesternBrainCells, CulturedEmbryo, MammalianHumansIsoelectric FocusingMice, KnockoutNeuroblastomaNeuronsPhosphatidylinositol 3-KinasesPhosphorylationProtein IsoformsProto-Oncogene Proteins c-aktPTEN PhosphohydrolasePhosphatidylinositol 3-KinasesProtein IsoformsProto-Oncogene Proteins c-aktPTEN PhosphohydrolaseAkt PKBbraincapillary isoelectric focusing, phosphorylationcell signalinggrowth factorsneuronsphosphatase and tensin homolog (PTEN)post-translational modification (PTM)

Identifiers

PMID26945062
PMCPMC4858973
OpenAlexW2289872273

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.