Evidence map›Paper›PMID 21327077›Full record

ArticleNucleus (Austin, Tex.)

Phosphorylation of nucleoporins: signal transduction-mediated regulation of their interaction with nuclear transport receptors.

Hidetaka Kosako, Naoko Imamoto

Open access · hybridAbstract read
In one paragraph

Article in Nucleus (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Molecular Crowing in Nuclear Pore.Sub-cellular biochemistry · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review
  8. Review
  9. Article
  10. Article
  11. Protein phosphatases at the nuclear envelope.Biochemical Society transactions · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. NSort/DB: an intranuclear compartment protein database.Genomics, proteomics & bioinformatics · 2012
    Article
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 2 institutions in 1 country.

Hidetaka KosakoDivision of Disease Proteomics; Institute for Enzyme Research; The University of Tokushima; Tokushima, Japan. kosako@ier.tokushima-u.ac.jp
Naoko Imamoto
RIKEN Advanced Science Institute · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nuclear pore complex (NPC) is composed of ∼30 unique proteins, collectively referred to as nucleoporins or Nups. While metazoan Nups are known to be phosphorylated during mitosis to cause disassembly of the NPC, what is less clear is whether Nups are phosphorylated and regulated by extracellular stimuli in interphase cells. Our multi-step phosphoproteomic approach revealed a number of physiologically relevant extracellular signal-regulated kinase (ERK) targets, including Nups containing FG repeats (FG Nups) that provide binding sites for nuclear transport receptors (NTRs) during the NPC passage. The phosphorylation of FG Nups by ERK does not affect the overall architecture of the NPC but directly inhibits their interactions with NTRs and regulates the permeability barrier properties of the NPC. Such regulation at the levels of transport machinery is expected to have a broad impact on cellular physiology through the spatiotemporal control of signaling events. Until recently, many studies have focused on cellular signaling-mediated phosphorylation of individual cargo proteins, such as transcription factors. An understanding of the effects of signaling pathways on nucleocytoplasmic transport machinery is only beginning to emerge.

Indexed as

Animalsbeta KaryopherinsExtracellular Signal-Regulated MAP KinasesHeLa CellsHumansInterphaseNuclear Pore Complex ProteinsPhosphorylationRNA InterferenceSignal Transductionbeta KaryopherinsExtracellular Signal-Regulated MAP KinasesNuclear Pore Complex ProteinsERKFG NupFG repeatimportin-βMAP kinaseNPCnuclear transport receptornucleocytoplasmic transportnucleoporinphosphorylation

Identifiers

PMID21327077
PMCPMC3027037
OpenAlexW2010552175

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.