Evidence map›Paper›PMID 25790465›Full record

ArticlePloS one2015

Nuclear envelope protein Lem2 is required for mouse development and regulates MAP and AKT kinases.

Olga Tapia, Loren G Fong, Michael D Huber, Stephen G Young, Larry Gerace

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. 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
1.2field-weighted citation impact, top 21% 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, 38 citations in OpenAlex.

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  6. Altered Expression ofInternational journal of molecular sciences · 2022
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  9. The Diverse Cellular Functions of Inner Nuclear Membrane Proteins.Cold Spring Harbor perspectives in biology · 2021
    Review
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  12. Review
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  15. Article
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

Olga TapiaDepartment of Cell and Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, California 92037, United States of America.
Loren G FongDepartment of Medicine, University of California Los Angeles, Los Angeles, California 90095, United States of America.
Michael D HuberDepartment of Cell and Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, California 92037, United States of America.
Stephen G YoungDepartment of Medicine, University of California Los Angeles, Los Angeles, California 90095, United States of America; Department of Human Genetics, University of California Los Angeles, Los Angeles, California 90095, United States of America.
Larry GeraceDepartment of Cell and Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, California 92037, United States of America.
Scripps Research Institute · USUniversity of California, Los Angeles · US

Funding

STRUCTURE AND FUNCTIONS OF THE NUCLEAR ENVELOPER01GM028521 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GERACE, LARRY R. · 1985 to 2020
$7.0M
San Diego Skeletal Muscle Research CenterP30AR061303 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHEN, JU · 2011 to 2015
$3.3M
New Therapeutic Approaches for Hutchinson-Gilford Progeria SyndromeR01HL086683 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FONG, LOREN GI · 2007 to 2011
$2.2M
CaaX Protein Processing and Human DiseaseR01AG035626 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI YOUNG, STEPHEN G. · 2009 to 2013
$2.0M
Protein Prenylation and ProgeriaR01HL089781 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FONG, LOREN GI · 2009 to 2013
$1.9M
NHLBI NIH HHS HL086683NHLBI NIH HHS HL089781NHLBI NIH HHS R01 HL086683NHLBI NIH HHS R01 HL089781NIAMS NIH HHS AR061303NIAMS NIH HHS P30 AR061303NIA NIH HHS AG035626NIA NIH HHS R01 AG035626NIGMS NIH HHS GM028521NIGMS NIH HHS R01 GM028521
6 · The paper itself

Abstract

The nuclear lamina, along with associated nuclear membrane proteins, is a nexus for regulating signaling in the nucleus. Numerous human diseases arise from mutations in lamina proteins, and experimental models for these disorders have revealed aberrant regulation of various signaling pathways. Previously, we reported that the inner nuclear membrane protein Lem2, which is expressed at high levels in muscle, promotes the differentiation of cultured myoblasts by attenuating ERK signaling. Here, we have analyzed mice harboring a disrupted allele for the Lem2 gene (Lemd2). No gross phenotypic defects were seen in heterozygotes, although muscle regeneration induced by cardiotoxin was delayed. By contrast, homozygous Lemd2 knockout mice died by E11.5. Although many normal morphogenetic hallmarks were observed in E10.5 knockout embryos, most tissues were substantially reduced in size. This was accompanied by activation of multiple MAP kinases (ERK1/2, JNK, p38) and AKT. Knockdown of Lem2 expression in C2C12 myoblasts also led to activation of MAP kinases and AKT. These findings indicate that Lemd2 plays an essential role in mouse embryonic development and that it is involved in regulating several signaling pathways. Since increased MAP kinase and AKT/mTORC signaling is found in other animal models for diseases linked to nuclear lamina proteins, LEMD2 should be considered to be another candidate gene for human disease.

Indexed as

Embryonic DevelopmentSignal TransductionAnimalsGene Knockout TechniquesMembrane ProteinsMiceMice, KnockoutMitogen-Activated Protein KinasesMutationNuclear ProteinsProto-Oncogene Proteins c-aktLem2 protein, mouseMembrane ProteinsMitogen-Activated Protein KinasesNuclear ProteinsProto-Oncogene Proteins c-akt

Identifiers

PMID25790465
PMCPMC4366207
OpenAlexW2070164440

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.