Evidence map›Paper›PMID 10594058›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1999

Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor.

K Ye, D A Compton, M M Lai, L D Walensky, S H Snyder

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

27 citing papers in PubMed, 64 citations in OpenAlex.

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  7. Inositol Hexakisphosphate Kinase-2 in Cerebellar Granule Cells Regulates Purkinje Cells and Motor Coordination via Protein 4.1N.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  8. 4.1N is involved in a flotillin-1/β-catenin/Wnt pathway and suppresses cell proliferation and migration in non-small cell lung cancer cell lines.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    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 3 institutions in 1 country.

K YeDepartments of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
D A Compton
M M Lai
L D Walensky
S H Snyder
Johns Hopkins Medicine · USDartmouth College · USJohns Hopkins University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007309 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI COX, ANDREA L · 1985 to 2019
$43.2M
NEUROCHEMICAL ACTIONS OF PSYCHOTROPIC DRUGSR37MH018501 · NIMH · JOHNS HOPKINS UNIVERSITY · PI SNYDER, SOLOMON H. · 1990 to 2009
$11.5M
NEUROCHEMICAL ACTIONS OF PSYCHOTROPIC DRUGSR01MH018501 · NIMH · JOHNS HOPKINS UNIVERSITY · PI SNYDER, SOLOMON H. · 1985 to 2019
$10.8M
Organization of the Mammalian Mitotic SpindleR37GM051542 · NIGMS · DARTMOUTH COLLEGE · PI COMPTON, DUANE A. · 2013 to 2022
$6.7M
Organization of the Mammilian Mitotic SpindleR01GM051542 · NIGMS · DARTMOUTH COLLEGE · PI COMPTON, DUANE A. · 1996 to 2012
$4.6M
NEUROTRANSMITTER RECEPTORSK05DA000074 · NIDA · JOHNS HOPKINS UNIVERSITY · PI SNYDER, SOLOMON H. · 1985 to 2009
$1.3M
NIDA NIH HHS DA-00074NIDA NIH HHS K05 DA000074NIGMS NIH HHS GM-07309NIGMS NIH HHS R01 GM051542NIGMS NIH HHS R37 GM051542NIGMS NIH HHS T32 GM007309NIMH NIH HHS MH18501NIMH NIH HHS R01 MH018501NIMH NIH HHS R37 MH018501
6 · The paper itself

Abstract

Protein 4.1N is a neuronal selective isoform of the erythrocyte membrane cytoskeleton protein 4.1R. In the present study, we demonstrate an interaction between 4.1N and nuclear mitotic apparatus protein (NuMA), a nuclear protein required for mitosis. The binding involves the C-terminal domain of 4.1N. In PC12 cells treatment with nerve growth factor (NGF) elicits translocation of 4. 1N to the nucleus and promotes its association with NuMA. Specific targeting of 4.1N to the nucleus arrests PC12 cells at the G1 phase and produces an aberrant nuclear morphology. Inhibition of 4.1N nuclear translocation prevents the NGF-mediated arrest of cell division, which can be reversed by overexpression of 4.1N. Thus, nuclear 4.1N appears to mediate the antiproliferative actions of NGF by antagonizing the role of NuMA in mitosis.

Indexed as

Membrane ProteinsAnimalsBiological TransportCell Cycle ProteinsCell DivisionCell NucleusCytoskeletal ProteinsG1 PhaseNerve Growth FactorNeuropeptidesNuclear ProteinsPC12 CellsRatsCell Cycle ProteinsCytoskeletal Proteinserythrocyte membrane protein band 4.1-like 1Membrane ProteinsNerve Growth FactorNeuropeptidesNuclear ProteinsNuma1 protein, rat

Identifiers

PMID10594058
PMCPMC6784956
OpenAlexW2142078007

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.