Evidence map›Paper›PMID 29382863›Full record

ArticleScientific reports2018

Visualization of human karyopherin beta-1/importin beta-1 interactions with protein partners in mitotic cells by co-immunoprecipitation and proximity ligation assays.

Laura Di Francesco, Annalisa Verrico, Italia Anna Asteriti, Paola Rovella, Pietro Cirigliano, Giulia Guarguaglini, Maria Eugenia Schininà, Patrizia Lavia

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Laura Di FrancescoDipartimento di Scienze Biochimiche, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185, Rome, Italy.
Annalisa VerricoInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, Via degli Apuli 4, 00185, Rome, Italy.
Italia Anna AsteritiInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, Via degli Apuli 4, 00185, Rome, Italy.
Paola RovellaInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, Via degli Apuli 4, 00185, Rome, Italy.
Pietro CiriglianoNikon Instruments S.p.A., Campi Bisenzio, Italy.
Giulia GuarguagliniInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, Via degli Apuli 4, 00185, Rome, Italy.
Maria Eugenia SchininàDipartimento di Scienze Biochimiche, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185, Rome, Italy. eugenia.schinina@uniroma1.it.
Patrizia LaviaInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, Via degli Apuli 4, 00185, Rome, Italy. patrizia.lavia@uniroma1.it.ORCID http://orcid.org/0000-0003-3310-6701
Institute of Molecular Biology and Pathology · ITBambino Gesù Children's Hospital · ITSapienza University of Rome · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Karyopherin beta-1/Importin beta-1 is a conserved nuclear transport receptor, acting in protein nuclear import in interphase and as a global regulator of mitosis. These pleiotropic functions reflect its ability to interact with, and regulate, different pathways during the cell cycle, operating as a major effector of the GTPase RAN. Importin beta-1 is overexpressed in cancers characterized by high genetic instability, an observation that highlights the importance of identifying its partners in mitosis. Here we present the first comprehensive profile of importin beta-1 interactors from human mitotic cells. By combining co-immunoprecipitation and proteome-wide mass spectrometry analysis of synchronized cell extracts, we identified expected (e.g., RAN and SUMO pathway factors) and novel mitotic interactors of importin beta-1, many with RNA-binding ability, that had not been previously associated with importin beta-1. These data complement interactomic studies of interphase transport pathways. We further developed automated proximity ligation assay (PLA) protocols to validate selected interactors. We succeeded in obtaining spatial and temporal resolution of genuine importin beta-1 interactions, which were visualized and localized in situ in intact mitotic cells. Further developments of PLA protocols will be helpful to dissect importin beta-1-orchestrated pathways during mitosis.

Indexed as

Mitosisbeta KaryopherinsBiological AssayHeLa CellsHumansImage Processing, Computer-AssistedImmunoprecipitationPolymerase Chain ReactionProtein Interaction Domains and Motifsbeta KaryopherinsKPNB1 protein, human

Identifiers

PMID29382863
PMCPMC5789818
OpenAlexW2807328335

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.