Evidence map›Paper›PMID 28576472›Full record

ArticleJournal of molecular biology2017

Redirecting SR Protein Nuclear Trafficking through an Allosteric Platform.

Brandon E Aubol, Kendra L Hailey, Laurent Fattet, Patricia A Jennings, Joseph A Adams

Abstract read
In one paragraph

Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
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  6. Article
  7. Enzymatic Noncovalent Synthesis.Chemical reviews · 2020
    Review
  8. Article
  9. Redox-dependent gating of VDAC by mitoNEET.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Article
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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

5 authors at 1 institution in 1 country.

Brandon E AubolDepartment of Pharmacology, University of California, San Diego, La Jolla, CA 92093-0636, USA.
Kendra L HaileyDepartment of Chemistry & Biochemistry, University of California, San Diego, La Jolla, CA 92093-0636, USA.
Laurent FattetDepartment of Pharmacology, University of California, San Diego, La Jolla, CA 92093-0636, USA.
Patricia A JenningsDepartment of Chemistry & Biochemistry, University of California, San Diego, La Jolla, CA 92093-0636, USA.
Joseph A AdamsDepartment of Pharmacology, University of California, San Diego, La Jolla, CA 92093-0636, USA. Electronic address: j2adams@ucsd.edu.
University of California, San Diego · US

Funding

Role of protein phosphorylation in RNA splicingR01GM067969 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ADAMS, JOSEPH · 2004 to 2024
$6.4M
Clk Kinases and Splicing RegulationR01GM098528 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ADAMS, JOSEPH · 2012 to 2019
$2.5M
NIGMS NIH HHS R01 GM067969NIGMS NIH HHS R01 GM098528
6 · The paper itself

Abstract

Although phosphorylation directs serine-arginine (SR) proteins from nuclear storage speckles to the nucleoplasm for splicing function, dephosphorylation paradoxically induces similar movement, raising the question of how such chemical modifications are balanced in these essential splicing factors. In this new study, we investigated the interaction of protein phosphatase 1 (PP1) with the SR protein splicing factor (SRSF1) to understand the foundation of these opposing effects in the nucleus. We found that RNA recognition motif 1 (RRM1) in SRSF1 binds PP1 and represses its catalytic function through an allosteric mechanism. Disruption of RRM1-PP1 interactions reduces the phosphorylation status of the RS domain in vitro and in cells, redirecting SRSF1 in the nucleus. The data imply that an allosteric SR protein-phosphatase platform balances phosphorylation levels in a "goldilocks" region for the proper subnuclear storage of an SR protein splicing factor.

Indexed as

Protein Processing, Post-TranslationalAllosteric RegulationBinding SitesCell NucleusHeLa CellsHumansPhosphorylationProtein BindingProtein ConformationReceptors, Neuropeptide YSerine-Arginine Splicing Factorsneuropeptide Y4 receptorReceptors, Neuropeptide YSerine-Arginine Splicing FactorsSRSF1 protein, humankinasekineticsphosphatasephosphorylationSR protein

Identifiers

PMID28576472
PMCPMC5536852
OpenAlexW2618575830

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.