Evidence map›Paper›PMID 20204506›Full record

ArticleNeurochemical research2011

Light-induced tyrosine phosphorylation of rod outer segment membrane proteins regulate the translocation, membrane binding and activation of type II α phosphatidylinositol-5-phosphate 4-kinase.

Zhong Huang, Robert E Anderson, Wei Cao, Allan F Wiechmann, Raju V S Rajala

Abstract read
In one paragraph

Article in Neurochemical research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Ribosomal targeting strategy and nuclear labeling to analyze photoreceptor phosphoinositide signatures.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2022
    Article
  3. Article
  4. Article
  5. Review
  6. 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 3 institutions in 2 countries.

Zhong HuangDepartment of Ophthalmology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
Robert E Anderson
Wei Cao
Allan F Wiechmann
Raju V S Rajala
University of Oklahoma Health Sciences Center · USDean McGee Eye Institute · USShenzhen University · CN

Funding

UNDERSTANDING THE ROLE OF RETINOL DEHYDROGENASES RDH11 AND RDH12 IN VISIONP20RR017703 · NCRR · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI CERESA, BRIAN P. · 2002 to 2011
$23.6M
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
NCRR NIH HHS P20 RR017703NCRR NIH HHS RR17703NEI 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

Type II phosphatidylinositol 5-phosphate 4-kinase (PIPKIIα) catalyzes the synthesis of phosphatidylinositol-4,5-bisphosphate (PI-4,5-P(2)), an essential lipid second messenger that may be involved in the regulation of phototransduction, neuroprotection, and morphogenesis in the vertebrate retina. Here we report that in rodent and transgenic frogs, the light-mediated activity and membrane binding of PIPKIIα in rod outer segments (ROS) is dependent on tyrosine phosphorylation of ROS proteins. The greater type II α PIP kinase activity in the light-adapted ROS membrane results from light-driven translocation of PIPKIIα from the rod inner segment to ROS, and subsequent binding to the ROS membrane, thus improving access of the kinase to its lipid substrates. These results indicate a novel mechanism of light regulation of the PIPKIIα activity in photoreceptors, and suggest that the greater PIPKIIα activity in light-adapted animals and the resultant accumulation of PI-4,5-P(2) within the ROS membrane may be important for the function of photoreceptor cells.

Indexed as

LightAnimalsAnimals, Genetically ModifiedBase SequenceCell LineDNA PrimersImmunohistochemistryMembrane ProteinsMicePhosphorylationPhosphotransferases (Alcohol Group Acceptor)Protein TransportRatsRats, Sprague-DawleyRod Cell Outer SegmentTyrosine1-phosphatidylinositol-4-phosphate 5-kinaseDNA PrimersMembrane ProteinsPhosphotransferases (Alcohol Group Acceptor)Tyrosine

Identifiers

PMID20204506
PMCPMC4227407
OpenAlexW1968886069

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.