Evidence map›Paper›PMID 16319169›Full record

ArticleMolecular biology of the cell2006

Regulated cellular partitioning of SR protein-specific kinases in mammalian cells.

Jian-Hua Ding, Xiang-Yang Zhong, Jonathan C Hagopian, Marissa M Cruz, Gourisankar Ghosh, James Feramisco, Joseph A Adams, Xiang-Dong Fu

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

72 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. Review
  3. CMGC Kinases in Viral Infection and Human Disease.Pathogens (Basel, Switzerland) · 2026
    Review
  4. Article
  5. SRSF1 interactome determined by proximity labeling reveals direct interaction with spliceosomal RNA helicase DDX23.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review

12 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 1 institution in 1 country.

Jian-Hua DingDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093-0651, USA.
Xiang-Yang Zhong
Jonathan C Hagopian
Marissa M Cruz
Gourisankar Ghosh
James Feramisco
Joseph A Adams
Xiang-Dong Fu
University of California San Diego · US

Funding

GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
Role of protein phosphorylation in RNA splicingR01GM067969 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ADAMS, JOSEPH · 2004 to 2024
$6.4M
Regulation of RNA metabolism and cell growth control by SR protein kinasesR01GM052872 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DOWDY, STEVEN F · 1996 to 2019
$5.4M
NIGMS NIH HHS GM-07752NIGMS NIH HHS GM-52872NIGMS NIH HHS R01 GM052872NIGMS NIH HHS R01 GM067969NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

Reversible phosphorylation of the SR family of splicing factors plays an important role in pre-mRNA processing in the nucleus. Interestingly, the SRPK family of kinases specific for SR proteins is localized in the cytoplasm, which is critical for nuclear import of SR proteins in a phosphorylation-dependent manner. Here, we report molecular dissection of the mechanism involved in partitioning SRPKs in the cytoplasm. Common among all SRPKs, the bipartite kinase catalytic core is separated by a unique spacer sequence. The spacers in mammalian SRPK1 and SRPK2 share little sequence homology, but they function interchangeably in restricting the kinases in the cytoplasm. Removal of the spacer in SRPK1 had little effect on the kinase activity, but it caused a quantitative translocation of the kinase to the nucleus and consequently induced aggregation of splicing factors in the nucleus. Rather than carrying a nuclear export signal as suggested previously, we found multiple redundant signals in the spacer that act together to anchor the kinase in the cytoplasm. Interestingly, a cell cycle signal induced nuclear translocation of the kinase at the G2/M boundary. These findings suggest that SRPKs may play an important role in linking signaling to RNA metabolism in higher eukaryotic cells.

Indexed as

Active Transport, Cell NucleusAnimalsCell NucleusHeLa CellsHumansInterphaseKineticsNuclear ProteinsPhosphorylationProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesProtein Sorting SignalsRNARNA-Binding ProteinsRNA SplicingSerine-Arginine Splicing FactorsNuclear ProteinsProtein Serine-Threonine KinasesProtein Sorting SignalsRNARNA-Binding ProteinsSerine-Arginine Splicing FactorsSRPK1 protein, humanSRPK2 protein, human

Identifiers

PMID16319169
PMCPMC1356596
OpenAlexW2130131426

What OpenQuestion holds

Textmetadata
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Registered trials

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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.