Evidence map›Paper›PMID 27802161›Full record

ArticleJournal of cell science2016

ELYS regulates the localization of LBR by modulating its phosphorylation state.

Yasuhiro Mimura, Masatoshi Takagi, Michaela Clever, Naoko Imamoto

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2016. 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
1.7field-weighted citation impact, top 15% 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, 34 citations in OpenAlex.

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  10. Dephosphorylation in nuclear reassembly after mitosis.Frontiers in cell and developmental biology · 2022
    Review
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  16. The Journal of biological chemistry · 2020
    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

4 authors at 1 institution in 1 country.

Yasuhiro MimuraCellular Dynamics Laboratory, Riken, Saitama 351-0198, Japan.
Masatoshi TakagiCellular Dynamics Laboratory, Riken, Saitama 351-0198, Japan.
Michaela CleverCellular Dynamics Laboratory, Riken, Saitama 351-0198, Japan.
Naoko ImamotoCellular Dynamics Laboratory, Riken, Saitama 351-0198, Japan nimamoto@riken.jp.ORCID 0000-0002-2886-3022
University of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lamin B receptor (LBR), an inner nuclear membrane (INM) protein, contributes to the functional integrity of the nucleus by tethering heterochromatin to the nuclear envelope. We have previously reported that the depletion of embryonic large molecule derived from yolk sac (ELYS; also known as AHCTF1), a component of the nuclear pore complex, from cells perturbs the localization of LBR to the INM, but little is known about the underlying molecular mechanism. In this study, we found that the depletion of ELYS promoted LBR phosphorylation at the residues known to be phosphorylated by cyclin-dependent kinase (CDK) and serine/arginine protein kinases 1 and 2 (SRPK1 and SRPK2, respectively). These phosphorylation events were most likely to be counter-balanced by protein phosphatase 1 (PP1), and the depletion of PP1 from cells consistently caused the mislocalization of LBR. These observations point to a new mechanism regulating the localization of LBR, which is governed by an ELYS-mediated phosphorylation network. This phosphorylation-dependent coordination between INM proteins and the nuclear pore complex might be important for the integrity of the nucleus.

Indexed as

Amino Acid SequenceCDC2 Protein KinaseChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneDNA-Binding ProteinsHEK293 CellsHeLa CellsHistonesHumansLamin B ReceptorLamin Type BMutationNuclear EnvelopeNuclear ProteinsPhosphorylationProtein DomainsAHCTF1 protein, humanCDC2 Protein KinaseChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneDNA-Binding ProteinsHistonesLamin B ReceptorLamin Type BNuclear ProteinsProtein IsoformsProtein Phosphatase 1Protein Serine-Threonine KinasesReceptors, Cytoplasmic and NuclearTranscription FactorsInner nuclear membrane proteinNuclear envelopeNuclear pore complexNucleoporinPhosphorylation

Identifiers

PMID27802161
PMCPMC5117198
OpenAlexW2528205526

What OpenQuestion holds

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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.