Evidence map›Paper›PMID 33306092›Full record

ArticleThe Journal of cell biology2021

An APEX2 proximity ligation method for mapping interactions with the nuclear lamina.

Joseph R Tran, Danielle I Paulson, James J Moresco, Stephen A Adam, John R Yates, Robert D Goldman, Yixian Zheng

Abstract read
In one paragraph

Article in The Journal of cell biology, 2021. 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
–field-weighted citation impact
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.

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  16. CTCF supports preferentially short lamina-associated domains.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2022
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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.

Joseph R TranCarnegie Institution for Science, Department of Embryology, Baltimore, MD.
Danielle I PaulsonCarnegie Institution for Science, Department of Embryology, Baltimore, MD.
James J MorescoThe Scripps Research Institution, Department of Molecular Medicine, La Jolla, CA.
Stephen A AdamNorthwestern University, Feinberg School of Medicine, Department of Cell and Developmental Biology, Chicago, IL.
John R YatesThe Scripps Research Institution, Department of Molecular Medicine, La Jolla, CA.
Robert D GoldmanNorthwestern University, Feinberg School of Medicine, Department of Cell and Developmental Biology, Chicago, IL.
Yixian ZhengCarnegie Institution for Science, Department of Embryology, Baltimore, MD.

Funding

TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI YATES III, JOHN R · 2012 to 2021
$20.7M
Super-resolution microscopy of nuclear lamin and spindle envelope/matrix functionR01GM106023 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI GOLDMAN, ROBERT D, ZHENG, YIXIAN · 2013 to 2020
$3.5M
Mechanisms of chromosome segregation and mitotic timingR01GM110151 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI ZHENG, YIXIAN · 2015 to 2018
$1.5M
NIGMS NIH HHS P41 GM103533NIGMS NIH HHS R01 GM106023NIGMS NIH HHS R01 GM110151
6 · The paper itself

Abstract

The nuclear lamina (NL) is a meshwork found beneath the inner nuclear membrane. The study of the NL is hindered by the insolubility of the meshwork and has driven the development of proximity ligation methods to identify the NL-associated/proximal proteins, RNA, and DNA. To simplify and improve temporal labeling, we fused APEX2 to the NL protein lamin-B1 to map proteins, RNA, and DNA. The identified NL-interacting/proximal RNAs show a long 3' UTR bias, a finding consistent with an observed bias toward longer 3' UTRs in genes deregulated in lamin-null cells. A C-rich motif was identified in these 3' UTR. Our APEX2-based proteomics identifies a C-rich motif binding regulatory protein that exhibits altered localization in lamin-null cells. Finally, we use APEX2 to map lamina-associated domains (LADs) during the cell cycle and uncover short, H3K27me3-rich variable LADs. Thus, the APEX2-based tools presented here permit identification of proteomes, transcriptomes, and genome elements associated with or proximal to the NL.

Indexed as

Protein Interaction Mapping3' Untranslated RegionsBase SequenceDNA-(Apurinic or Apyrimidinic Site) LyaseEndonucleasesHCT116 CellsHEK293 CellsHumansK562 CellsLamin Type BMultifunctional EnzymesNuclear LaminaProtein DomainsProteomeRNARNA Splicing3' Untranslated RegionsAPEX2 protein, humanDNA-(Apurinic or Apyrimidinic Site) LyaseEndonucleasesLamin Type BMultifunctional EnzymesProteomeRNA

Identifiers

PMID33306092
PMCPMC7737704

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Registered trials

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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.