Evidence map›Paper›PMID 33758005›Full record

ArticleLife science alliance2021

Mapping the micro-proteome of the nuclear lamina and lamina-associated domains.

Xianrong Wong, Jevon A Cutler, Victoria E Hoskins, Molly Gordon, Anil K Madugundu, Akhilesh Pandey, Karen L Reddy

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 51 citations in OpenAlex.

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  8. The role of inner nuclear membrane protein emerin in myogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
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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

7 authors at 2 institutions in 3 countries.

Xianrong WongDepartment of Biological Chemistry, Johns Hopkins University of Medicine, Baltimore, MD, USA.ORCID 0000-0002-1995-7043
Jevon A CutlerDepartment of Biological Chemistry, Johns Hopkins University of Medicine, Baltimore, MD, USA.
Victoria E HoskinsDepartment of Biological Chemistry, Johns Hopkins University of Medicine, Baltimore, MD, USA.
Molly GordonDepartment of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Anil K MadugunduDepartment of Biological Chemistry, Johns Hopkins University of Medicine, Baltimore, MD, USA.ORCID 0000-0003-4274-7316
Akhilesh PandeyDepartment of Biological Chemistry, Johns Hopkins University of Medicine, Baltimore, MD, USA.
Karen L ReddyDepartment of Biological Chemistry, Johns Hopkins University of Medicine, Baltimore, MD, USA kreddy4@jhmi.edu.ORCID 0000-0003-4548-5999
Johns Hopkins University · USAgency for Science, Technology and Research · SG

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
Predoctoral Training Program in Human GeneticsT32GM007814 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VALLE, DAVID · 1985 to 2021
$10.6M
Differential Regulation and Roles of A-type Lamins in Early G1R01GM132427 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI REDDY, KAREN LYNN, WILSON, KATHERINE L · 2020 to 2023
$2.4M
Differential Protein Interactions in Hutchinson-Gilford Progeria SyndromeR21AG050132 · NIA · JOHNS HOPKINS UNIVERSITY · PI REDDY, KAREN LYNN · 2016 to 2017
$446k
NIA NIH HHS R21 AG050132NIGMS NIH HHS R01 GM132427NIGMS NIH HHS T32 GM007445NIGMS NIH HHS T32 GM007814
6 · The paper itself

Abstract

The nuclear lamina is a proteinaceous network of filaments that provide both structural and gene regulatory functions by tethering proteins and large domains of DNA, the so-called lamina-associated domains (LADs), to the periphery of the nucleus. LADs are a large fraction of the mammalian genome that are repressed, in part, by their association to the nuclear periphery. The genesis and maintenance of LADs is poorly understood as are the proteins that participate in these functions. In an effort to identify proteins that reside at the nuclear periphery and potentially interact with LADs, we have taken a two-pronged approach. First, we have undertaken an interactome analysis of the inner nuclear membrane bound LAP2β to further characterize the nuclear lamina proteome. To accomplish this, we have leveraged the BioID system, which previously has been successfully used to characterize the nuclear lamina proteome. Second, we have established a system to identify proteins that bind to LADs by developing a chromatin-directed BioID system. We combined the BioID system with the m6A-tracer system which binds to LADs in live cells to identify both LAD proximal and nuclear lamina proteins. In combining these datasets, we have further characterized the protein network at the nuclear lamina, identified putative LAD proximal proteins and found several proteins that appear to interface with both micro-proteomes. Importantly, several proteins essential for LAD function, including heterochromatin regulating proteins related to H3K9 methylation, were identified in this study.

Indexed as

AnimalsCell LineCell NucleusChromatinDNADNA-Binding ProteinsGenomeHeterochromatinHumansMembrane ProteinsMiceNIH 3T3 CellsNuclear LaminaNuclear ProteinsProtein BindingProtein DomainsChromatinDNADNA-Binding ProteinsHeterochromatinlamina-associated polypeptide 2Membrane ProteinsNuclear ProteinsProteome

Identifiers

PMID33758005
PMCPMC8008952
OpenAlexW3137466286

What OpenQuestion holds

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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.