Evidence map›Paper›PMID 23077346›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2012

Short RNA molecules with high binding affinity to the KH motif of A-kinase anchoring protein 1 (AKAP1): implications for the regulation of steroidogenesis.

Petar N Grozdanov, Douglas M Stocco

Open access · bronzeAbstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

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  17. ACTH Action on StAR Biology.Frontiers in neuroscience · 2016
    Review
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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

2 authors at 1 institution in 1 country.

Petar N GrozdanovDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, Texas 79430, USA.
Douglas M Stocco
Texas Tech University Health Sciences Center · US

Funding

MITOCHONDRIAL PROTEINS AND LEYDIG CELL STEROIDOGENESISR37HD017481 · NICHD · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI STOCCO, DOUGLAS M · 1996 to 2005
$1.9M
MITOCHONDRIAL PROTEINS AND LEYDIG CELL STEROIDOGENESISR01HD017481 · NICHD · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI STOCCO, DOUGLAS M · 1985 to 2011
$1.5M
NICHD NIH HHS HD-17481NICHD NIH HHS R01 HD017481NICHD NIH HHS R37 HD017481
6 · The paper itself

Abstract

One of the key regulators of acute steroid hormone biosynthesis in steroidogenic tissues is the steroidogenic acute regulatory (STAR) protein. Acute regulation of STAR production on the transcriptional level is mainly achieved through a cAMP-dependent mechanism, which is well understood. However, less is known about the posttranscriptional regulation of STAR synthesis, specifically the factors influencing the destiny of the Star mRNA after it leaves the nucleus. Here, we show that the 3'-untranslated region of Star mRNA interacts with the heterogeneous nuclear ribonucleoprotein K-homology (KH) motif of the mitochondrial scaffold A-kinase anchoring protein 1 (AKAP1) in vitro with a moderate affinity as measured by EMSAs. A mutation that mimics the phosphorylation state of the KH motif at a specific serine either did not alter, or had a negative impact on, protein-RNA binding under these conditions. The KH motif of AKAP1 binds short pyrimidine-rich RNA molecules with a stable hairpin structure as demonstrated by in vitro selection. AKAP1 also interacts with STAR mRNA in a dibutyryl-cAMP-stimulated human steroidogenic adrenocortical carcinoma cell line in vivo. Therefore, we propose a model in which AKAP1 anchors Star mRNA at the mitochondria, thus stabilizing the translational complex at this organelle, a situation that might affect STAR production and steroidogenesis. In addition, we suggest that the last 216 amino acid residues of AKAP1 might participate in the degradation of STAR and other nuclear-encoded mitochondrial mRNAs through interaction with a RNA-induced silencing complex, specifically with the argonaute 2 protein.

Indexed as

Phosphoproteins3' Untranslated RegionsA Kinase Anchor ProteinsAmino Acid MotifsAmino Acid SequenceArgonaute ProteinsCell Line, TumorDNA-Binding ProteinsGonadal Steroid HormonesHeterogeneous-Nuclear Ribonucleoprotein KHumansMitochondriaMolecular Sequence DataPhosphorylationPromoter Regions, GeneticRibonucleoproteins3' Untranslated RegionsAKAP1 protein, humanA Kinase Anchor ProteinsArgonaute ProteinsDNA-Binding ProteinsGonadal Steroid HormonesHeterogeneous-Nuclear Ribonucleoprotein KHNRNPK protein, humanPhosphoproteinsRibonucleoproteinsRNA, MessengerSteroidogenic Acute Regulatory Protein

Identifiers

PMID23077346
PMCPMC3517713
OpenAlexW2090881230

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.