ArticleBiochimica et biophysica acta2009
Reduced expression of A-type lamins and emerin activates extracellular signal-regulated kinase in cultured cells.
Article in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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.
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.
Who cites it
37 citing papers in PubMed, 67 citations in OpenAlex.
- Nuclear envelope proteins in cancer: revisiting the significance of LEM-domain proteins.Frontiers in cell and developmental biology · 2026Review
- The role of inner nuclear membrane proteins in tumourigenesis and as potential targets for cancer therapy.Cancer metastasis reviews · 2022Review
- Cytoplasmic keratins couple with and maintain nuclear envelope integrity in colonic epithelial cells.Molecular biology of the cell · 2022Article
- Molecular Pathology of Laminopathies.Annual review of pathology · 2022Review
- The Role of Emerin in Cancer Progression and Metastasis.International journal of molecular sciences · 2021Review
- Review
- Consequences ofCells · 2020Article
- Two novel cases further expand the phenotype of TOR1AIP1-associated nuclear envelopathies.Human genetics · 2020Article
- Simulated Microgravity Reduces Focal Adhesions and Alters Cytoskeleton and Nuclear Positioning Leading to Enhanced Apoptosis via Suppressing FAK/RhoA-Mediated mTORC1/NF-κB and ERK1/2 Pathways.International journal of molecular sciences · 2018Article
- Protein sequestration at the nuclear periphery as a potential regulatory mechanism in premature aging.The Journal of cell biology · 2018Review
- Defective Nuclear Lamina in Aneuploidy and Carcinogenesis.Frontiers in oncology · 2018Review
- Spindle associated membrane protein 1 (Samp1) is required for the differentiation of muscle cells.Scientific reports · 2017Article
- Article
- MAPK signaling pathways and HDAC3 activity are disrupted during differentiation of emerin-null myogenic progenitor cells.Disease models & mechanisms · 2017Article
- Causes and consequences of nuclear envelope alterations in tumour progression.European journal of cell biology · 2016Review
- Diseases of the Nucleoskeleton.Comprehensive Physiology · 2016Review
- Deleterious assembly of the lamin A/C mutant p.S143P causes ER stress in familial dilated cardiomyopathy.Journal of cell science · 2016Article
- Analysis of Nuclear Lamina Proteins in Myoblast Differentiation by Functional Complementation.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Review
- Nuclear membrane diversity: underlying tissue-specific pathologies in disease?Current opinion in cell biology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
backgroundMutations in genes encoding A-type lamins and emerin cause cardiomyopathy and muscular dystrophy. We previously showed activation of the extracellular signal-regulated kinase (ERK) branch of the mitogen-activated protein kinase (MAPK) cascade in hearts of mice with mutations in these genes. Here, we tested the hypothesis that reducing A-type lamins and emerin in cultured cells activate ERK signaling.
methodsWe used siRNA to knockdown A-type lamins and emerin in HeLa and C2C12 cells. Activation of ERK was assessed by immunoblotting and immunofluorescence microscopy with antibodies against phosphorylated protein and by using real-time RT-PCR to measure RNAs encoded by genes for transcription factors stimulated by ERK.
resultsKnockdown of A-type lamins and emerin in HeLa and C2C12 stimulated phosphorylation and nuclear translocation of ERK as well as activation of genes encoding downstream transcription factors. A MAPK/ERK kinase (MEK) inhibitor reduced ERK phosphorylation in cells with reduced expression of A-type lamins and emerin.
conclusionsThese results provide proof for the hypothesis that altered expression of emerin and A-type lamins activates ERK signaling, which in turn can cause cardiomyopathy. GENERAL SIGNIFICANCE: ERK is a potential target for the pharmacological treatment of cardiomyopathy caused by mutations in the genes encoding emerin and A-type lamins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.