Evidence map›Paper›PMID 12851456›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein.

Jiuyong Xie, Ji-Ann Lee, Tracy L Kress, Kimberly L Mowry, Douglas L Black

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

100 citing papers in PubMed, 178 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. PARN Maintains RNA Stability to Regulate Insulin Maturation and GSIS in Pancreatic β Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  8. Review
  9. Modulation of DBiomedicines · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. PTBP1 Positively Regulates the Translation of Circadian Clock Gene,International journal of molecular sciences · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. Article

40 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

5 authors at 3 institutions in 1 country.

Jiuyong XieHoward Hughes Medical Institute, Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, CA 90095-1662, USA.
Ji-Ann Lee
Tracy L Kress
Kimberly L Mowry
Douglas L Black
Howard Hughes Medical Institute · USBrown University · USUniversity of California, Los Angeles · US

Funding

The Regulation of Neuronal Exon SplicingR01GM049662 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BLACK, DOUGLAS L · 1998 to 2019
$6.5M
RNA LOCALIZATION IN XENOPUS OOCYTESR01HD030699 · NICHD · BROWN UNIVERSITY · PI MOWRY, KIMBERLY L · 1993 to 2003
$1.0M
NICHD NIH HHS R01 HD030699NICHD NIH HHS R01 HD30699NIGMS NIH HHS R01 GM049662NIGMS NIH HHS R01 GM49662
6 · The paper itself

Abstract

The heterogeneous nuclear ribonucleoprotein particle (hnRNP) proteins play important roles in mRNA processing in eukaryotes, but little is known about how they are regulated by cellular signaling pathways. The polypyrimidine-tract binding protein (PTB, or hnRNP I) is an important regulator of alternative pre-mRNA splicing, of viral RNA translation, and of mRNA localization. Here we show that the nucleo-cytoplasmic transport of PTB is regulated by the 3',5'-cAMP-dependent protein kinase (PKA). PKA directly phosphorylates PTB on conserved Ser-16, and PKA activation in PC12 cells induces Ser-16 phosphorylation. PTB carrying a Ser-16 to alanine mutation accumulates normally in the nucleus. However, export of this mutant protein from the nucleus is greatly reduced in heterokaryon shuttling assays. Conversely, hyperphosphorylation of PTB by coexpression with the catalytic subunit of PKA results in the accumulation of PTB in the cytoplasm. This accumulation is again specifically blocked by the S16A mutation. Similarly, in Xenopus oocytes, the phospho-Ser-16-PTB is restricted to the cytoplasm, whereas the non-Ser-16-phosphorylated PTB is nuclear. Thus, direct PKA phosphorylation of PTB at Ser-16 modulates the nucleo-cytoplasmic distribution of PTB. This phosphorylation likely plays a role in the cytoplasmic function of PTB.

Indexed as

3T3 CellsActive Transport, Cell NucleusAmino Acid SequenceAnimalsBinding SitesCell LineCyclic AMP-Dependent Protein KinasesFemaleHeLa CellsHumansIn Vitro TechniquesMiceMolecular Sequence DataOocytesPhosphorylationPolypyrimidine Tract-Binding ProteinCyclic AMP-Dependent Protein KinasesPolypyrimidine Tract-Binding ProteinRecombinant ProteinsSerine

Identifiers

PMID12851456
PMCPMC166389
OpenAlexW2129670085

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.