Evidence map›Paper›PMID 18823366›Full record

ArticleJournal of neurochemistry2008

Activation and membrane binding of retinal protein kinase Balpha/Akt1 is regulated through light-dependent generation of phosphoinositides.

Guiyuan Li, Ammaji Rajala, Allan F Wiechmann, Robert E Anderson, Raju V S Rajala

Open access · greenAbstract read
In one paragraph

Article in Journal of neurochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

29 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Girdin: A Class I Phosphatidylinositol 3-Kinase-Binding Protein in the Retina.Advances in experimental medicine and biology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The Enigmatic Role of Lipids in Cilia Signaling.Frontiers in cell and developmental biology · 2020
    Review
  9. Article
  10. Redundant and Nonredundant Functions of Akt Isoforms in the Retina.Advances in experimental medicine and biology · 2018
    Article
  11. The Effects of Metformin on Obesity-Induced Dysfunctional Retinas.Investigative ophthalmology & visual science · 2017
    Article
  12. Article
  13. High-Fat Diet-Induced Retinal Dysfunction.Investigative ophthalmology & visual science · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Insulin receptor signaling in cones.The Journal of biological chemistry · 2013
    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

5 authors at 2 institutions in 1 country.

Guiyuan LiDepartments of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA.
Ammaji Rajala
Allan F Wiechmann
Robert E Anderson
Raju V S Rajala
Dean McGee Eye Institute · USUniversity of Oklahoma Health Sciences Center · US

Funding

SECOND MESSENGERS IN THE RETINAR01EY000871 · NEI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI RAJALA, RAJU VS · 1985 to 2020
$7.2M
CORE--MOLECULAR BIOLOGYP30EY012190 · NEI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI ANDERSON, ROBERT E · 1999 to 2009
$5.2M
Light Activation of Retinal Insulin Receptor SignalingR01EY016507 · NEI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI RAJALA, RAJU VS · 2006 to 2013
$2.7M
NEI NIH HHS EY00871NEI NIH HHS EY016507NEI NIH HHS EY12190NEI NIH HHS P30 EY012190NEI NIH HHS R01 EY000871NEI NIH HHS R01 EY016507
6 · The paper itself

Abstract

Akt is a phospholipid-binding protein and the downstream effector of the phosphoinositide 3-kinase (PI3K) pathway. Akt has three isoforms: Akt1, Akt2, and Akt3. All of these isoforms are expressed in rod photoreceptor cells, but the individual functions of each isoform are not known. In this study, we found that light induces the activation of Akt1. The membrane binding of Akt1 to rod outer segments (ROS) is insulin receptor (IR)/PI3K-dependent as demonstrated by reduced binding of Akt1 to ROS membranes of photoreceptor-specific IR knockout mice. Membrane binding of Akt1 is mediated through its Pleckstrin homology (PH) domain. To determine whether binding of the PH domain of Akt1 to photoreceptor membranes is regulated by light, various green fluorescent protein (GFP)/Akt1-PH domain fusion proteins were expressed in rod photoreceptors of transgenic Xenopus laevis under the control of the Xenopus opsin promoter. The R25C mutant PH domain of Akt1, which does not bind phosphoinositides, failed to associate with plasma membranes in a light-dependent manner. This study suggests that light-dependent generation of phosphoinositides regulates the activation and membrane binding of Akt1 in vivo. Our results also suggest that actin cytoskeletal organization may be regulated through light-dependent generation of phosphoinositides.

Indexed as

AnimalsAnimals, Genetically ModifiedAnimals, NewbornCell MembraneChromonesEnzyme ActivationEnzyme InhibitorsFemaleGene Expression RegulationHumansHypoglycemic AgentsInsulinLightMaleMiceMice, Knockout2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-oneAkt1 protein, ratChromonesEnzyme InhibitorsHypoglycemic AgentsInsulinMorpholinesPhosphatidylinositolsProto-Oncogene Proteins c-aktReceptor, Insulin

Identifiers

PMID18823366
PMCPMC2596869
OpenAlexW1968716331

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.