Evidence map›Paper›PMID 19116344›Full record

ArticleEndocrinology2009

Akt2 regulation of Cdc2-like kinases (Clk/Sty), serine/arginine-rich (SR) protein phosphorylation, and insulin-induced alternative splicing of PKCbetaII messenger ribonucleic acid.

Kun Jiang, Niketa A Patel, James E Watson, Hercules Apostolatos, Eden Kleiman, Olivia Hanson, Masatoshi Hagiwara, Denise R Cooper

Open access · greenAbstract read
In one paragraph

Article in Endocrinology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
2.2field-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

61 citing papers in PubMed, 83 citations in OpenAlex.

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1 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

8 authors at 5 institutions in 2 countries.

Kun JiangDepartment of Molecular Medicine, University of South Florida College of Medicine, Tampa, Florida 33612, USA.
Niketa A Patel
James E Watson
Hercules Apostolatos
Eden Kleiman
Olivia Hanson
Masatoshi Hagiwara
Denise R Cooper
James A. Haley Veterans' Hospital · USFlorida College · USTokyo Medical and Dental University · JPUniversity of Central Oklahoma · USUniversity of South Florida · US

Funding

Insulin Signaling Pathways Regulating PKCBeta SplicingR01DK054393 · NIDDK · UNIVERSITY OF SOUTH FLORIDA · PI COOPER, DENISE RATZLAFF · 2001 to 2011
$2.6M
NIDDK NIH HHS DK54393NIDDK NIH HHS R01 DK054393
6 · The paper itself

Abstract

Serine/arginine-rich (SR) proteins play essential roles in the constitutive and regulated splicing of precursor mRNAs. Phosphorylation of the arginine/serine dipeptide-rich (RS) domain by SR protein kinases such as Cdc2-like kinases (Clk/Sty) modulates their subcellular localization and activation. However, it remains unclear how these kinases and their target SR proteins are regulated by extracellular signals. Regulation of protein kinase C betaII (PKCbetaII) pre-mRNA alternative splicing via exon inclusion by Akt2, a central kinase in insulin action, involves phosphorylation of SR proteins. Here we showed that Akt2, in response to insulin, resulted in phosphorylation of Clk/Sty, which then altered SR protein phosphorylation in concert with Akt2. Insulin-stimulated PKCbetaII pre-mRNA splicing was blocked by Clk/Sty and phosphatidylinositol-3-kinase inhibitors, and diabetic Akt2-null mouse tissues had impaired phospho-Clk/Sty, SR protein phosphorylation, and PKCbetaII expression. Furthermore, we observed that Akt2 phosphorylated several SR proteins distinct from Clk/Sty in response to insulin. Akt2-catalyzed phosphorylation of Clk/Sty and SR proteins revealed a role for both kinases in splicing regulation indicating dual functions for Akt2 in response to insulin in this pathway.

Indexed as

Alternative SplicingAnimalsCells, CulturedChlorocebus aethiopsCOS CellsInsulinMiceMice, KnockoutModels, BiologicalNuclear ProteinsPhosphorylationProtein Kinase CProtein Kinase C betaProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene Proteins c-aktClk dual-specificity kinasesInsulinNuclear ProteinsProtein Kinase CProtein Kinase C betaProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene Proteins c-aktRNA-Binding ProteinsRNA, MessengerSerine-Arginine Splicing Factors

Identifiers

PMID19116344
PMCPMC2671910
OpenAlexW2010994336

What OpenQuestion holds

Textmetadata
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.