The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
The inner nuclear membrane protein Emerin regulates β‐catenin activity by restricting its accumulation in the nucleus
Open accessAbstract
Emerin is a type II inner nuclear membrane (INM) protein of unknown function. Emerin function is likely to be important because, when it is mutated, emerin promotes both skeletal muscle and heart defects. Here we show that one function of Emerin is to regulate the flux of beta-catenin, an important transcription coactivator, into the nucleus. Emerin interacts with beta-catenin through a conserved adenomatous polyposis coli (APC)-like domain. When GFP-emerin is expressed in HEK293 cells, beta-catenin is restricted to the cytoplasm and beta-catenin activity is inhibited. In contrast, expression of an emerin mutant, lacking its APC-like domain (GFP-emerinDelta), dominantly stimulates beta-catenin activity and increases nuclear accumulation of beta-catenin. Human fibroblasts that are null for emerin have an autostimulatory growth phenotype. This unusual growth phenotype arises through enhanced nuclear accumulation and activity of beta-catenin and can be replicated in wild-type fibroblasts by transfection with constitutively active beta-catenin. Our results support recent findings that suggest that INM proteins can influence signalling pathways by restricting access of transcription coactivators to the nucleus.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Emerin is a structural integral protein which acts to stabilize chromatin and regulate gene expression [108].”
From DNA repair deficiency and senescence in concussed professional athletes involved in contact sports (2019) · cites this paper as [108]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Activation of β-Catenin-Tcf Signaling in Colon Cancer by Mutations in β-Catenin or APC
Morin, P. J., Sparks, A. B., Kořínek, V., Barker, N., Clevers, H. C., Vogelstein, B., & Kinzler, K. W. (1997) · Science · doi:10.1126/science.275.5307.1787 · Cited by 4,000
Self-citationFunctional interaction of β-catenin with the transcription factor LEF-1
Behrens, J., von Kries, J. P., Kühl, M., Bruhn, L., Wedlich, D., Grosschedl, R., & Birchmeier, W. (1996) · Nature · doi:10.1038/382638a0 · Cited by 2,912
A role for Wnt signalling in self-renewal of haematopoietic stem cells
Reya, T., Duncan, A. W., Ailles, L., Domen, J., Scherer, D. C., Willert, K., Hintz, L., Nusse, R., & Weissman, I. L. (2003) · Nature · doi:10.1038/nature01593 · Cited by 2,159
The β-Catenin/TCF-4 Complex Imposes a Crypt Progenitor Phenotype on Colorectal Cancer Cells
van de Wetering, M., Sancho, E., Verweij, C., de Lau, W., Oving, I., Hurlstone, A., van der Horn, K., Batlle, E., Coudreuse, D., Haramis, A.-P., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)01014-0 · Cited by 2,030
Self-citationXTcf-3 Transcription Factor Mediates β-Catenin-Induced Axis Formation in Xenopus Embryos
Molenaar, M., van de Wetering, M., Oosterwegel, M., Peterson-Maduro, J., Godsave, S., Korinek, V., Roose, J., Destrée, O., & Clevers, H. (1996) · Cell · doi:10.1016/s0092-8674(00)80112-9 · Cited by 1,824
Self-citationMutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy
Bonne, G., di Barletta, M. R., Varnous, S., Bécane, H. M., Hammouda, E.-H., Merlini, L., Muntoni, F., Greenberg, C. R., Gary, F., Urtizberea, J. A., et al. (1999) · Nature Genetics · doi:10.1038/6799 · Cited by 1,384
Fatkin, D., MacRae, C. A., Sasaki, T., Wolff, M. R., Porcu, M., Frenneaux, M. P., Atherton, J. J., Vidaillet, H. J., Jr., Spudich, S., Girolami, U. D., et al. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912023412302 · Cited by 1,366
Loss of a-Type Lamin Expression Compromises Nuclear Envelope Integrity Leading to Muscular Dystrophy
Sullivan, T. L., Escalante‐Alcalde, D., Bhatt, H., Anver, M. R., Bhat, N. R., Nagashima, K., Stewart, C. L., & Burke, B. E. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.5.913 · Cited by 1,224
Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy
Bione, S., Maestrini, E., Rivella, S., Mancini, M., Regis, S., Romeo, G., & Toniolo, D. (1994) · Nature Genetics · doi:10.1038/ng1294-323 · Cited by 913
Identification of essential genes in cultured mammalian cells using small interfering RNAs
Harborth, J., Elbashir, S. M., Bechert, K., Tuschl, T., & Weber, K. K. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.24.4557 · Cited by 828
Cited by
Sorted by citations
Cellular Mechanotransduction: From Tension to Function
Martino, F. D., Perestrelo, A. R., Vinarský, V., Pagliari, S., & Forte, G. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00824 · Cited by 1,028
Gruenbaum, Y., & Foisner, R. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034115 · Cited by 565
Zhang, Q., Bethmann, C., Worth, N. F., Davies, J. D., Wasner, C., Feuer, A., Ragnauth, C. D., Yi, Q., Mellad, J. A., Warren, D. T., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm238 · Cited by 556
Self-citationDynamics and interplay of nuclear architecture, genome organization, and gene expressionPreprint
Schneider, R., & Grosschedl, R. (2007) · Genes & Development · doi:10.1101/gad.1604607 · Cited by 434
When Lamins Go Bad: Nuclear Structure and Disease
Schreiber, K. H., & Kennedy, B. K. (2013) · Cell · doi:10.1016/j.cell.2013.02.015 · Cited by 407
Metadata
- Authors
- Markiewicz, E., Tilgner, K., Barker, N., van de Wetering, M., Clevers, H., Dorobek, M., Hausmanowa‐Petrusewicz, I., Ramaekers, F. C., Broers, J. L., Blankesteijn, W. M., Salpingidou, G., Wilson, R. G., Ellis, J. A., & Hutchison, C. J.
- Affiliations
- Durham University (GB)
- Hubrecht Institute for Developmental Biology and Stem Cell Research (NL)
- Polish Academy of Sciences (PL)
- Maastricht University (NL)
- James Cook University Hospital (GB)
- King's College London (GB)
- Corresponding author
- Hutchison, Christopher J
- ORCID
- Venue
- The EMBO Journal
- Published
- 2006-07-20
- Volume
- 25
- Issue
- 14
- Pages
- 3275-3285
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1523183
- OpenAlex
- W2115754063
- Cited by
- 246
- References
- 57
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 6 · 2023: 5 · 2022: 10 · 2021: 10 · 2020: 15 · 2019: 10 · 2018: 13 · 2017: 12 · 2016: 17 · 2015: 16 · 2014: 18 · 2013: 13 · 2012: 17
- FWCI
- 5.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- TU/e Research Portal (publishedVersion)
- Durham Research Online (Durham University) (acceptedVersion)
- TU/e Research Portal (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Durham Research Online (Durham University) (submittedVersion)
- Durham Research Online (Durham University) (submittedVersion, cc-by)
- Research Portal (King's College London) (submittedVersion)
- KNAW Research Portal (The Royal Netherlands Academy of Arts and Sciences) (submittedVersion)
- Newcastle University ePrints (Newcastle Univesity)
- Funders
- Wellcome Trust
- Royal Society
- Muscular Dystrophy UK
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Connexins and lens biology
- Keywords
- emerin, inner nuclear membrane, β-catenin, nuclear accumulation, transcriptional coactivator, nuclear trafficking, Wnt signaling
- MeSH terms
- Cell Line, Cells, Cultured, Humans, Membrane Proteins, Nuclear Envelope, Nuclear Proteins, Thymopoietins, Signal Transduction, Trans-Activators, Muscular Dystrophy, Emery-Dreifuss, beta Catenin
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
