Evidence map›Paper›PMID 16314522›Full record

ArticleMolecular and cellular biology2005

Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor.

Dipak K Giri, Mohamed Ali-Seyed, Long-Yuan Li, Dung-Fang Lee, Pin Ling, Geoffrey Bartholomeusz, Shao-Chun Wang, Mien-Chie Hung

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

121 citing papers in PubMed, 245 citations in OpenAlex.

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  13. An Insight into Molecular Targets of Breast Cancer Brain Metastasis.International journal of molecular sciences · 2022
    Review
  14. Dihydroconiferyl Ferulate Isolated fromPharmaceuticals (Basel, Switzerland) · 2022
    Article
  15. Article
  16. Article
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61 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.

Dipak K GiriDepartment of Molecular and Cellular Oncology, University of Texas MD Anderson Cancer Center, Houston, 77030, USA.
Mohamed Ali-Seyed
Long-Yuan Li
Dung-Fang Lee
Pin Ling
Geoffrey Bartholomeusz
Shao-Chun Wang
Mien-Chie Hung
The University of Texas MD Anderson Cancer Center · US

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Kathrin Milbury · 1985 to 2026
$290.8M
Tyrosine Kinase-Dependant and - Independent Pathways of EGFR in Breast Cancer ProP01CA099031 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI HUNG, MIEN-CHIE · 2003 to 2014
$11.6M
Tumor Progression of Nuclear EGFR in Breast CancerR01CA109311 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI HUNG, MIEN-CHIE · 2004 to 2014
$3.0M
NCI NIH HHS CA16672NCI NIH HHS P01 CA099031NCI NIH HHS P30 CA016672NCI NIH HHS R01 CA109311
6 · The paper itself

Abstract

The cell membrane receptor ErbB-2 migrates to the nucleus. However, the mechanism of its nuclear translocation is unclear. Here, we report a novel mechanism of its nuclear localization that involves interaction with the transport receptor importin beta1, nuclear pore protein Nup358, and a host of players in endocytic internalization. Knocking down importin beta1 using small interfering RNA oligonucleotides or inactivation of small GTPase Ran by RanQ69L, a dominant-negative mutant of Ran, causes a nuclear transport defect of ErbB-2. Mutation of a putative nuclear localization signal in ErbB-2 destroys its interaction with importin beta1 and arrests nuclear translocation, while inactivation of nuclear export receptor piles up ErbB-2 within the nucleus. Additionally, blocking of internalization by a dominant-negative mutant of dynamin halts its nuclear localization. Thus, the cell membrane-embedded ErbB-2, through endocytosis using the endocytic vesicle as a vehicle, importin beta1 as a driver and Nup358 as a traffic light, migrates from the cell surface to the nucleus. This novel mechanism explains how a receptor tyrosine kinase on the cell surface can be translocated into the nucleus. This pathway may serve as a general mechanism to allow direct communication between cell surface receptors and the nucleus, and our findings thus open a new era in understanding direct trafficking between the cell membrane and nucleus.

Indexed as

EndocytosisActive Transport, Cell Nucleusbeta KaryopherinsCell NucleusCells, CulturedClathrinEndosomesErb-b2 Receptor Tyrosine KinasesExportin 1 ProteinHumansKaryopherinsMolecular ChaperonesMutationNuclear Localization SignalsNuclear Pore Complex Proteinsran GTP-Binding Proteinbeta KaryopherinsClathrinErb-b2 Receptor Tyrosine KinasesExportin 1 ProteinKaryopherinsKPNB1 protein, humanMolecular ChaperonesNuclear Localization SignalsNuclear Pore Complex Proteinsran-binding protein 2ran GTP-Binding ProteinReceptors, Cell SurfaceReceptors, Cytoplasmic and Nuclear

Identifiers

PMID16314522
PMCPMC1316946
OpenAlexW2139577140

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.