Evidence map›Paper›PMID 16481405›Full record

ArticleMolecular biology of the cell2006

Factors controlling fibroblast growth factor receptor-1's cytoplasmic trafficking and its regulation as revealed by FRAP analysis.

Star M Dunham-Ems, Haridas E Pudavar, Jason M Myers, Pamela A Maher, Paras N Prasad, Michal K Stachowiak

Open access · greenAbstract 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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

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  10. Gene expression profiling analysis of castration-resistant prostate cancer.Medical science monitor : international medical journal of experimental and clinical research · 2015
    Article
  11. Review
  12. Article
  13. Sorting of the FGF receptor 1 in a human glioma cell line.Histochemistry and cell biology · 2013
    Article
  14. Article
  15. 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

6 authors at 2 institutions in 1 country.

Star M Dunham-EmsMolecular and Structural Neurobiology and Gene Therapy Program, Department of Pathology and Anatomical Sciences, State University of New York at Buffalo, Buffalo, NY 14214, USA.
Haridas E Pudavar
Jason M Myers
Pamela A Maher
Paras N Prasad
Michal K Stachowiak
University at Buffalo, State University of New York · USSalk Institute for Biological Studies · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biochemical and microscopic studies have indicated that FGFR1 is a transmembrane and soluble protein present in the cytosol and nucleus. How FGFR1 enters the cytosol and subsequently the nucleus to control cell development and associated gene activities has become a compelling question. Analyses of protein synthesis, cytoplasmic subcompartmental distribution and movement of FGFR1-EGFP and FGFR1 mutants showed that FGFR1 exists as three separate populations (a) a newly synthesized, highly mobile, nonglycosylated, cytosolic receptor that is depleted by brefeldin A and resides outside the ER-Golgi lumen, (b) a slowly diffusing membrane receptor population, and (c) an immobile membrane pool increased by brefeldin A. RSK1 increases the highly mobile cytosolic FGFR1 population and its overall diffusion rate leading to increased FGFR1 nuclear accumulation, which coaccumulates with RSK1. A model is proposed in which newly synthesized FGFR1 can enter the (a) "nuclear pathway," where the nonglycosylated receptor is extruded from the pre-Golgi producing highly mobile cytosolic receptor molecules that rapidly accumulate in the nucleus or (b) "membrane pathway," in which FGFR1 is processed through the Golgi, where its movement is spatially restricted to trans-Golgi membranes with limited lateral mobility. Entrance into the nuclear pathway is favored by FGFR1's interaction with kinase active RSK1.

Indexed as

Protein BiosynthesisAnimalsBrefeldin ACattleCell NucleusCells, CulturedCytoplasmFluorescence Recovery After PhotobleachingGolgi ApparatusGreen Fluorescent ProteinsHumansModels, BiologicalProtein TransportReceptor, Fibroblast Growth Factor, Type 1Recombinant Fusion ProteinsRibosomal Protein S6 Kinases, 90-kDaBrefeldin Aenhanced green fluorescent proteinGreen Fluorescent ProteinsReceptor, Fibroblast Growth Factor, Type 1Recombinant Fusion ProteinsRibosomal Protein S6 Kinases, 90-kDaRPS6KA1 protein, human

Identifiers

PMID16481405
PMCPMC1446089
OpenAlexW2108057299

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.