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.
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
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?
Emerin is a structural integral protein that stabilizes chromatin and regulates gene expression.
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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 3,983 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationFatkin, 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 1,354 · see citing works
Mutations 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., Francesco Muntoni, A., Greenberg, C. R., Gary, F., Urtizberea, J. A., et al. (1999) · Nature Genetics · doi:10.1038/6799 · Cited by 1,353 · see citing works
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. K., Nagashima, K., Stewart, C. L., & Burke, B. E. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.5.913 · Cited by 1,197 · see citing works
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 886 · see citing works
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 · see citing works
Nuclear-cytoplasmic shuttling of APC regulates β-catenin subcellular localization and turnover
Henderson, B. R. (2000) · Nature Cell Biology · doi:10.1038/35023605 · Cited by 475 · see citing works
di Barletta, M. R., Ricci, E., Galluzzi, G., Tonali, P. A., Mora, M., Morandi, L. O., Romorini, A., Voït, T., Ørstavik, K. H., Merlini, L., et al. (2000) · The American Journal of Human Genetics · doi:10.1086/302869 · Cited by 415 · see citing works
Self-citationStockinger, A., Eger, A., Wolf, J., Beug, H., & Foisner, R. (2001) · Journal of Cell Biology · doi:10.1083/jcb.200104036 · Cited by 380 · see citing works
The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein
Manilal, S. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.6.801 · Cited by 380 · see citing works
The APC tumour suppressor has a nuclear export function
Rosin-Arbesfeld, R., Townsley, F., & Bienz, M. (2000) · Nature · doi:10.1038/35023016 · Cited by 343 · cited 2× · see citing works
“A number of studies have shown that APC shuttles between the nucleus and cytoplasm (Henderson, 2000; Neufeld et al, 2000; Rosin-Arbesfeld et al, 2000) through centrally located nuclear export signal sequences (Rosin-Arbesfeld et al, 2003) and mediates the CRM1-dependent nuclear export of b-catenin.”
BackgroundDistinct functional domains in emerin bind lamin A and DNA-bridging protein BAF
Lee, K. K., Haraguchi, T., Lee, R. S., Koujin, T., Hiraoka, Y., & Wilson, K. L. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.24.4567 · Cited by 336 · see citing works
Lamins: building blocks or regulators of gene expression?
Hutchison, C. J. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm950 · Cited by 291 · see citing works
Self-citationJohnson, B. R., Nitta, R. T., Frock, R. L., Mounkes, L. C., Barbie, D. A., Stewart, C. L., Harlow, E., & Kennedy, B. K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403250101 · Cited by 282 · see citing works
Zhang, Q., Ragnauth, C. D., Skepper, J. N., Worth, N. F., Warren, D. T., Roberts, R. G., Weissberg, P. L., Ellis, J. A., & Shanahan, C. M. (2005) · Journal of Cell Science · doi:10.1242/jcs.01642 · Cited by 277 · see citing works
Self-citationNesprin‐1α self‐associates and binds directly to emerin and lamin A in vitro
Mislow, J. M. K., Holaska, J. M., Kim, M. S., Lee, K. K., Segura‐Totten, M., Wilson, K. L., & McNally, E. M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03105-8 · Cited by 260 · see citing works
Lamin A/C Binding Protein LAP2α Is Required for Nuclear Anchorage of Retinoblastoma Protein
Markiewicz, E., Dechat, T., Foisner, R., Quinlan, R. A., & Hutchison, C. J. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-07-0450 · Cited by 251 · see citing works
Self-citationDirect Interaction between Emerin and Lamin A
Clements, L. A., Manilal, S., Love, D. R., & Morris, G. E. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.2023 · Cited by 248 · see citing works
Both emerin and lamin C depend on lamin A for localization at the nuclear envelope
Vaughan, O. A., Alvarez-Reyes, M., Bridger, J. M., Broers, J. L. V., Ramaekers, F. C. S., Wehnert, M. S., Morris, G. E., Whitfield, W. G. F., & Hutchison, C. J. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.14.2577 · Cited by 236 · see citing works
Self-citationHolaska, J. M., Lee, K. K., Kowalski, A. K., & Wilson, K. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208811200 · Cited by 236 · see citing works
Holaska, J. M., Kowalski, A. K., & Wilson, K. L. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020231 · Cited by 233 · see citing works
Regulation of tumor suppressors by nuclear-cytoplasmic shuttling
Fabbro, M., & Henderson, B. R. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00019-8 · Cited by 231 · see citing works
Melcon, G., Kozlov, S. V., Cutler, D. A., Sullivan, T., Hernandez, L. F., Zhao, P., Mitchell, S., Nader, G. A., Bakay, M. A., Rottman, J. N., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi479 · Cited by 220 · see citing works
Brill, L. M., Salomon, A. R., Ficarro, S. B., Mukherji, M., Stettler‐Gill, M., & Peters, E. C. (2004) · Analytical Chemistry · doi:10.1021/ac035352d · Cited by 210 · see citing works
Liu, J., Lee, K. K., Segura‐Totten, M., Neufeld, E., Wilson, K. L., & Gruenbaum, Y. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0730821100 · Cited by 203 · see citing works
Padmakumar, V. C., Abraham, S., Braune, S. A., Noegel, A. A., Tunggal, B., Karakesisoglou, I., & Korenbaum, E. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.01.014 · Cited by 191 · see citing works
Nuclear-cytoplasmic shuttling of Axin regulates subcellular localization of β-catenin
Cong, F., & VARMUS, H. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307344101 · Cited by 189 · see citing works
Pan, D., Estévez-Salmerón, L. D., Stroschein, S. L., Zhu, X., He, J., Zhou, S., & Luo, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411234200 · Cited by 187 · see citing works
Nuclear export of the APC tumour suppressor controls β‐catenin function in transcription
Rosin‐Arbesfeld, R., Cliffe, A., Brabletz, T., & Bienz, M. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg105 · Cited by 179 · see citing works
Muchir, A., van Engelen, B. G. M., Lammens, M. M. Y., Mislow, J. M. K., McNally, E. M., Schwartz, K., & Bonne, G. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.07.002 · Cited by 177 · see citing works
BAF: roles in chromatin, nuclear structure and retrovirus integration
Segura‐Totten, M., & Wilson, K. L. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.03.004 · Cited by 176 · see citing works
APC‐mediated downregulation of β‐catenin activity involves nuclear sequestration and nuclear export
Neufeld, K. L., Zhang, F., Cullen, B. R., & White, R. L. (2000) · EMBO Reports · doi:10.1093/embo-reports/kvd117 · Cited by 174 · see citing works
Lamin A/C–dependent Localization of Nesprin-2, a Giant Scaffolder at the Nuclear Envelope
Libotte, T., Zaim, H., Abraham, S., Padmakumar, V. C., Schneider, M., Lu, W., Munck, M., Hutchison, C. J., Wehnert, M. S., Fahrenkrog, B., et al. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-11-1009 · Cited by 169 · see citing works
Self-citationOsada, S., Ohmori, S., & Taira, M. (2003) · Development · doi:10.1242/dev.00401 · Cited by 158 · see citing works
A-type lamins are essential for TGF-β1 induced PP2A to dephosphorylate transcription factors
van Berlo, J. H., Voncken, J. W., Kubben, N., Broers, J. L. V., Duisters, R. F. J. J., van Leeuwen, R. E. W., Crijns, H. J. G. M., Ramaekers, F. C. S., Hutchison, C. J., & Pinto, Y. M. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi316 · Cited by 152 · see citing works
Self-citationHaraguchi, T., Holaska, J. M., Yamane, M., Koujin, T., Hashiguchi, N., Mori, C., Wilson, K. L., & Hiraoka, Y. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04007.x · Cited by 149 · see citing works
Heart-specific localization of emerin: new insights into Emery-Dreifuss muscular dystrophy
Cartegni, L. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.13.2257 · Cited by 148 · see citing works
Margalit, A., Segura‐Totten, M., Gruenbaum, Y., & Wilson, K. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408364102 · Cited by 147 · see citing works
Shimi, T., Koujin, T., Segura‐Totten, M., Wilson, K. L., Haraguchi, T., & Hiraoka, Y. (2003) · Journal of Structural Biology · doi:10.1016/j.jsb.2003.11.013 · Cited by 145 · see citing works
Structural Characterization of the LEM Motif Common to Three Human Inner Nuclear Membrane Proteins
Laguri, C., Gilquin, B., Wolff, N., Lebrun, R., Courchay, K., Callebaut, I., Worman, H. J., & Zinn‐Justin, S. (2001) · Structure · doi:10.1016/s0969-2126(01)00611-6 · Cited by 125 · see citing works
A newly recognized autosomal dominant limb girdle muscular dystrophy with cardiac involvement
van der Kooi, A. J., Ledderhof, T. M., DEVOOGT, W., Res, J., Bouwsma, G., Troost, D., Busch, H. F. M., Becker, A. E., & deVisser, M. (1996) · Annals of Neurology · doi:10.1002/ana.410390513 · Cited by 119 · see citing works
CRM1- and Ran-independent nuclear export of β-catenin
Wiechens, N., & Fagotto, F. (2001) · Current Biology · doi:10.1016/s0960-9822(00)00045-2 · Cited by 107 · see citing works
Wnt signal transduction and the formation of the myocardium
Eisenberg, L. M., & Eisenberg, C. A. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.02.014 · Cited by 105 · see citing works
Drosophila α-Catenin and E-cadherin Bind to Distinct Regions of Drosophila Armadillo*
Pai, L., Kirkpatrick, C., Blanton, J., Oda, H., Takeichi, M., & Peifer, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.50.32411 · Cited by 97 · see citing works
Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts
Lattanzi, G., Cenni, V., Marmiroli, S., Capanni, C., Mattioli, E., Merlini, L., Squarzoni, S., & Maraldi, N. M. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00415-7 · Cited by 90 · see citing works
Nucleo-cytoplasmic Shuttling of Axin, a Negative Regulator of the Wnt-β-Catenin Pathway
Wiechens, N., Heinle, K., Englmeier, L., Schohl, A., & Fagotto, F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307253200 · Cited by 84 · see citing works
The expression, lamin-dependent localization and RNAi depletion phenotype for emerin inC. elegans
Gruenbaum, Y., Lee, K. K., Liu, J., Cohen, M., & Wilson, K. L. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.5.923 · Cited by 78 · see citing works
Wolff, N., Gilquin, B., Courchay, K., Callebaut, I., Worman, H. J., & Zinn‐Justin, S. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02649-7 · Cited by 75 · see citing works
Eleftheriou, A., Yoshida, M., & Henderson, B. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102656200 · Cited by 74 · see citing works
Hirano, Y., Segawa, M., Shinkai‐Ouchi, F., Yamakawa, Y., Furukawa, K., Takeyasu, K., & Horigome, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503214200 · Cited by 65 · see citing works
Markiewicz, E. (2002) · Journal of Structural Biology · doi:10.1016/s1047-8477(02)00573-7 · Cited by 52 · see citing works
Self-citationTsukahara, T., Tsujino, S., & Arahata, K. (2002) · Muscle & Nerve · doi:10.1002/mus.10085 · Cited by 42 · see citing works
Emerin expression in early development of Xenopus laevis
Gareiß, M., Eberhardt, K., Krüger, E., Kandert, S., Böhm, C., Zentgraf, H., Müller, C. R., & Dabauvalle, M. (2005) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2004.11.006 · Cited by 15 · see citing works
Flagged first, then by citations
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 958 · see citing works
Gruenbaum, Y., & Foisner, R. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034115 · Cited by 536 · see citing works
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 539 · see citing works
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 421 · see citing works
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 384 · see citing works
Progeria syndromes and ageing: what is the connection?
Burtner, C. R., & Kennedy, B. K. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2944 · Cited by 386 · see citing works
The nuclear envelope environment and its cancer connections
Chow, K.-H., Factor, R. E., & Ullman, K. S. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3219 · Cited by 361 · see citing works
Role of A-type lamins in signaling, transcription, and chromatin organization
Andrés, V., & González, J. M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200904124 · Cited by 289 · see citing works
Accessorizing and anchoring the LINC complex for multifunctionality
Chang, W., Worman, H. J., & Gundersen, G. G. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201409047 · Cited by 275 · see citing works
Nuclear lamins: key regulators of nuclear structure and activities
Prokocimer, M., Davidovich, M., Nissim‐Rafinia, M., Wiesel‐Motiuk, N., Bar, D. Z., Barkan, R., Meshorer, E., & Gruenbaum, Y. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00676.x · Cited by 272 · see citing works
Blurring the Boundary: The Nuclear Envelope Extends Its Reach
Stewart, C. L., Roux, K. J., & Burke, B. E. (2007) · Science · doi:10.1126/science.1142034 · Cited by 264 · see citing works
Lamin-binding ProteinsPreprint
Wilson, K. L., & Foisner, R. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000554 · Cited by 253 · see citing works
The Nuclear Envelope as a Signaling Node in Development and Disease
Dauer, W. T., & Worman, H. J. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.10.016 · Cited by 232 · see citing works
Lamins at the crossroads of mechanosignalingPreprint
Osmanagic‐Myers, S., Dechat, T., & Foisner, R. (2015) · Genes & Development · doi:10.1101/gad.255968.114 · Cited by 230 · see citing works
Lamin A/C Is a Risk Biomarker in Colorectal Cancer
Willis, N. D., Cox, T. R., Rahman-Casans, S. F. U., Smits, K. M., Przyborski, S. A., van den Brandt, P. A., van Engeland, M., Weijenberg, M. P., Wilson, R., A, A. P. D. B., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002988 · Cited by 229 · see citing works
Self-citationSalpingidou, G., Smertenko, A., Hausmanowa-Petrucewicz, I., Hussey, P. J., & Hutchison, C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702026 · Cited by 209 · see citing works
Self-citationNetworking in the nucleus: a spotlight on LEM-domain proteins
Barton, L. J., Soshnev, A. A., & Geyer, P. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.03.005 · Cited by 206 · see citing works
The nuclear envelope proteome differs notably between tissues
Korfali, N., Wilkie, G. S., Swanson, S. K., Sršeň, V., Heras, J. I. D. L., Batrakou, D. G., Malik, P. R., Zuleger, N., Kerr, A. R. W., Florens, L. A., et al. (2012) · Nucleus · doi:10.4161/nucl.22257 · Cited by 195 · see citing works
Cellular mechanosensing: Getting to the nucleus of it all
Fedorchak, G. R., Kaminski, A., & Lammerding, J. (2014) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2014.06.009 · Cited by 191 · see citing works
The nuclear envelope LEM-domain protein emerin
Berk, J. M., Tifft, K. E., & Wilson, K. L. (2013) · Nucleus · doi:10.4161/nucl.25751 · Cited by 186 · see citing works
Holaska, J. M., & Wilson, K. L. (2007) · Biochemistry · doi:10.1021/bi602636m · Cited by 181 · see citing works
Barrier-to-autointegration factor – a BAFfling little protein
Margalit, A., Brachner, A., Gotzmann, J., Foisner, R., & Gruenbaum, Y. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.02.004 · Cited by 174 · see citing works
Proteins that associate with lamins: Many faces, many functions
Schirmer, E. C., & Foisner, R. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.03.012 · Cited by 173 · see citing works
Demmerle, J., Koch, A. J., & Holaska, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.325308 · Cited by 168 · see citing works
Holaska, J. M., Rais‐Bahrami, S., & Wilson, K. L. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl423 · Cited by 167 · see citing works
Emery‐Dreifuss muscular dystrophy
Heller, S. A., Shih, R. S., Kalra, R., & Kang, P. B. (2019) · Muscle & Nerve · doi:10.1002/mus.26782 · Cited by 166 · see citing works
Oh, N. S., Lee, J. Y., Kim, Y.-T., Kim, S. H., & Lee, J.-H. (2020) · Gut Microbes · doi:10.1080/19490976.2020.1785803 · Cited by 166 · see citing works
The inner nuclear envelope as a transcription factor resting place
Heessen, S., & Fornerod, M. W. J. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401075 · Cited by 162 · see citing works
The nuclear envelope at a glance
Wilson, K. L., & Berk, J. M. (2010) · Journal of Cell Science · doi:10.1242/jcs.019042 · Cited by 158 · see citing works
LEM‐Domain Proteins: New Insights into Lamin‐Interacting Proteins
Wagner, N., & Krohne, G. (2007) · International review of cytology · doi:10.1016/s0074-7696(07)61001-8 · Cited by 157 · see citing works
Wnt3a-Induced Mesoderm Formation and Cardiomyogenesis in Human Embryonic Stem Cells
Tran, T. H., Wang, X., Browne, C., Zhang, Y., Schinke, M., Izumo, S., & Burcin, M. M. (2009) · Stem Cells · doi:10.1002/stem.95 · Cited by 145 · see citing works
Evolvement of LEM proteins as chromatin tethers at the nuclear periphery
Brachner, A., & Foisner, R. (2011) · Biochemical Society Transactions · doi:10.1042/bst20110724 · Cited by 140 · see citing works
Quantitative Analysis Reveals that Actin and Src-Family Kinases Regulate Nuclear YAP1 and Its Export
Ege, N., Dowbaj, A. M., Jiang, M., Howell, M. T., Hooper, S., Foster, C., Jenkins, R. P., & Sahai, E. A. (2018) · Cell Systems · doi:10.1016/j.cels.2018.05.006 · Cited by 131 · see citing works
TMEM43 mutations in emery‐dreifuss muscular dystrophy‐related myopathy
Liang, W., Mitsuhashi, H., Keduka, E., Nonaka, I., Noguchi, S., Nishino, I., & Hayashi, Y. K. (2010) · Annals of Neurology · doi:10.1002/ana.22338 · Cited by 129 · see citing works
Bertrand, A., Ziaei, S., Ehret, C., Duchemin, H., Mamchaoui, K., Bigot, A., Mayer, M., Quijano-Roy, S., Desguerre, I., Lainé, J., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.144907 · Cited by 126 · see citing works
Muchir, A., Pavlidis, P., Bonne, G., Hayashi, Y. K., & Worman, H. J. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm137 · Cited by 126 · see citing works
Semper, R. P., Mejías‐Luque, R., Groß, C. J., Anderl, F., Mueller, A., Vieth, M. W., Busch, D. H., da Costa, C. P., Ruland, J., Groß, O., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400362 · Cited by 121 · see citing works
Koch, A. J., & Holaska, J. M. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2013.12.008 · Cited by 114 · see citing works
Laminopathies and lamin‐associated signaling pathways
Maraldi, N. M., Capanni, C., Cenni, V., Fini, M., & Lattanzi, G. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22992 · Cited by 112 · see citing works
Causes and consequences of nuclear envelope alterations in tumour progression
Bell, E. S., & Lammerding, J. (2016) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2016.06.007 · Cited by 110 · see citing works
Laminopathies: The molecular background of the disease and the prospects for its treatment
Zaremba-Czogalla, M., Dubińska–Magiera, M., & Rzepecki, R. (2011) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-010-0038-9 · Cited by 103 · see citing works
The LINC complex and human disease
Meinke, P., Nguyen, T. D., & Wehnert, M. S. (2011) · Biochemical Society Transactions · doi:10.1042/bst20110658 · Cited by 100 · see citing works
Nuclear membrane diversity: underlying tissue-specific pathologies in disease?
Worman, H. J., & Schirmer, E. C. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.06.003 · Cited by 97 · see citing works
Lamins and lamin-associated proteins in aging and disease
Vlcek, S., & Foisner, R. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.04.001 · Cited by 94 · see citing works
Wnt signaling inside the nucleus
Shitashige, M., Hirohashi, S., & Yamada, T. (2008) · Cancer Science · doi:10.1111/j.1349-7006.2007.00716.x · Cited by 95 · see citing works
Wheeler, M., Davies, J. D., Zhang, Q., Emerson, L. J., Hunt, J. S., Shanahan, C. M., & Ellis, J. A. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.03.025 · Cited by 94 · see citing works
Self-citationCancer biology and the nuclear envelope: A convoluted relationship
Heras, J. I. D. L., Batrakou, D. G., & Schirmer, E. C. (2012) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2012.01.008 · Cited by 90 · see citing works
Tissue specificity in the nuclear envelope supports its functional complexity
Heras, J. I. D. L., Meinke, P., Batrakou, D. G., Sršeň, V., Zuleger, N., Kerr, A. R. W., & Schirmer, E. C. (2013) · Nucleus · doi:10.4161/nucl.26872 · Cited by 88 · see citing works
Bermeo, S., Vidal, C., Zhou, H., & Duque, G. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25185 · Cited by 83 · see citing works
Components and Mechanisms of Nuclear Mechanotransduction
Niethammer, P. (2021) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120319-030049 · Cited by 82 · see citing works
Lamin A/C and Emerin depletion impacts chromatin organization and dynamics in the interphase nucleus
Ranade, D., Pradhan, R., Jayakrishnan, M., Hegde, S., & Sengupta, K. (2019) · BMC Molecular and Cell Biology · doi:10.1186/s12860-019-0192-5 · Cited by 79 · see citing works
Emerin and the Nuclear Lamina in Muscle and Cardiac Disease
Holaska, J. M. (2008) · Circulation Research · doi:10.1161/circresaha.108.172197 · Cited by 80 · see citing works
Nesprin-2 Interacts with α-Catenin and Regulates Wnt Signaling at the Nuclear Envelope
Neumann, S., Schneider, M., Daugherty, R. L., Gottardi, C. J., Eming, S. A., Beijer, Å., Noegel, A. A., & Karakesisoglou, I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.119651 · Cited by 79 · see citing works
Tilgner, K., Wojciechowicz, K., Jahoda, C. A. B., Hutchison, C. J., & Markiewicz, E. (2009) · Journal of Cell Science · doi:10.1242/jcs.026179 · Cited by 80 · see citing works
Self-citationPekovic, V., & Hutchison, C. J. (2008) · Journal of Anatomy · doi:10.1111/j.1469-7580.2008.00928.x · Cited by 75 · see citing works
Self-citationLoregger, A., Grandl, M., Mejías‐Luque, R., Allgäuer, M., Degenhart, K., Haselmann, V., Oikonomou, C., Hatzis, P., Janssen, K., Nitsche, U., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aac6757 · Cited by 74 · see citing works
Dedeić, Z., Cetera, M., Cohen, T. V., & Holaska, J. M. (2011) · Journal of Cell Science · doi:10.1242/jcs.080259 · Cited by 72 · see citing works
The Nuclear Option: Evidence Implicating the Cell Nucleus in Mechanotransduction
Szczesny, S. E., & Mauck, R. L. (2016) · Journal of Biomechanical Engineering · doi:10.1115/1.4035350 · Cited by 72 · see citing works
Emery-Dreifuss muscular dystrophy
Muchir, A., & Worman, H. J. (2007) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-007-0025-3 · Cited by 70 · see citing works
Sun-mediated mechanical LINC between nucleus and cytoskeleton regulates βcatenin nuclear access
Uzer, G., Bas, G., Sen, B., Xie, Z., Birks, S., Olcum, M., McGrath, C., Styner, M., & Rubin, J. E. (2018) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2018.04.013 · Cited by 69 · see citing works
Role of Nuclear Lamins in Nuclear Organization, Cellular Signaling, and Inherited Diseases
Parnaik, V. K. (2008) · International review of cytology · doi:10.1016/s1937-6448(07)66004-3 · Cited by 67 · see citing works
Human tumour viruses and the deregulation of cell polarity in cancer
Banks, L., Pim, D., & Thomas, M. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3400 · Cited by 66 · see citing works
Loss of GATA6 Leads to Nuclear Deformation and Aneuploidy in Ovarian Cancer
Capo‐chichi, C. D., Cai, K. Q., Testa, J. R., Godwin, A. K., & Xu, X. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00087-09 · Cited by 67 · see citing works
Current insights into LMNA cardiomyopathies: Existing models and missing LINCs
Brayson, D., & Shanahan, C. M. (2017) · Nucleus · doi:10.1080/19491034.2016.1260798 · Cited by 66 · see citing works
Dour, C. L., Macquart, C., Sera, F., Homma, S., Bonne, G., Morrow, J., Worman, H. J., & Muchir, A. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw389 · Cited by 66 · see citing works
Reorganization of the nuclear lamina and cytoskeleton in adipogenesis
Verstraeten, V. L. R. M., Renes, J., Ramaekers, F. C. S., Kamps, M. A. F., Kuijpers, H. J. H., Verheyen, F., Wabitsch, M., Steijlen, P. M., Steensel, M. A. M. V., & Broers, J. L. V. (2011) · Histochemistry and Cell Biology · doi:10.1007/s00418-011-0792-4 · Cited by 66 · see citing works
Self-citationThe endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA cleavage in vivo
Brachner, A., Braun, J., Ghodgaonkar, M. M., Castor, D., Zlopaša, L., Ehrlich, V. A., Jiricny, J., Gotzmann, J., Knasmüller, S., & Foisner, R. (2012) · Journal of Cell Science · doi:10.1242/jcs.098392 · Cited by 62 · see citing works
Emerin intermolecular links to emerin and BAF
Berk, J. M., Simon, D. N., Jenkins-Houk, C., Westerbeck, J. W., Grønning-Wang, L. M., Carlson, C. R., & Wilson, K. L. (2014) · Journal of Cell Science · doi:10.1242/jcs.148247 · Cited by 61 · see citing works
The cancer-testis antigens SPANX-A/C/D and CTAG2 promote breast cancer invasion
Maine, E. A., Westcott, J. M., Prechtl, A. M., Dang, T. T., Whitehurst, A. W., & Pearson, G. W. (2016) · Oncotarget · doi:10.18632/oncotarget.7408 · Cited by 59 · see citing works
Lamina-Associated Polypeptide (LAP)2α and Other LEM Proteins in Cancer Biology
Brachner, A., & Foisner, R. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4899-8032-8_7 · Cited by 59 · see citing works
Tyrosine phosphorylation of nuclear-membrane protein emerin by Src, Abl and other kinases
Tifft, K. E., Little, K. A., & Wilson, K. L. (2009) · Journal of Cell Science · doi:10.1242/jcs.048397 · Cited by 59 · see citing works
Wong, X., & Stewart, C. L. (2020) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-121219-083616 · Cited by 56 · see citing works
Factors Affecting the Nuclear Localization of β‐Catenin in Normal and Malignant Tissue
Morgan, R. G., Ridsdale, J., Tonks, A., & Darley, R. L. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24803 · Cited by 56 · see citing works
Structure and unique mechanical aspects of nuclear lamin filaments
Kronenberg‐Tenga, R., & Medalia, O. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.06.017 · Cited by 56 · see citing works
WNT/β‐catenin pathway is a key regulator of cardiac function and energetic metabolism
Balatskyi, V. V., Sówka, A., Dobrzyń, P., & Piven, O. O. (2023) · Acta Physiologica · doi:10.1111/apha.13912 · Cited by 54 · see citing works
Genome-wide analysis links emerin to neuromuscular junction activity in Caenorhabditis elegans
González‐Aguilera, C., Ikegami, K., Ayuso, C., de Luis, A., Íñiguez, M., Cabello, J., Lieb, J. D., & Askjaer, P. (2014) · Genome biology · doi:10.1186/gb-2014-15-2-r21 · Cited by 54 · see citing works
Cell Mechanosensitivity Is Enabled by the LINC Nuclear Complex
Uzer, G., Rubin, C. T., & Rubin, J. E. (2016) · Current Molecular Biology Reports · doi:10.1007/s40610-016-0032-8 · Cited by 54 · see citing works
Role of the nuclear membrane protein Emerin in front-rear polarity of the nucleus
Nastały, P., Purushothaman, D., Marchesi, S., Poli, A., Lendenmann, T., Kidiyoor, G. R., Beznoussenko, G. V., Lavore, S., Romano, O. M., Dimos Poulikakos, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15910-9 · Cited by 53 · see citing works
The mechanical stability of proteins regulates their translocation rate into the cell nucleus
Infante, E., Stannard, A., Stephanie Board, Rico-Lastres, P., Rostkova, E. V., Beedle, A. E. M., Lezamiz, A., Wang, Y. J., Breen, S. G., Panagaki, F., et al. (2019) · Nature Physics · doi:10.1038/s41567-019-0551-3 · Cited by 51 · see citing works
The Diverse Cellular Functions of Inner Nuclear Membrane ProteinsPreprint
Pawar, S., & Kutay, U. (2021) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a040477 · Cited by 53 · see citing works
Hirschy, A., Croquelois, A., Perriard, E. R., Schoenauer, R., Agarkova, I., Hoerstrup, S. P., Taketo, M. M., Pedrazzini, T., Perriard, J., & Ehler, E. (2010) · Basic Research in Cardiology · doi:10.1007/s00395-010-0101-8 · Cited by 50 · see citing works
Emergence of TNIK inhibitors in cancer therapeutics
Yamada, T., & Masuda, M. (2017) · Cancer Science · doi:10.1111/cas.13203 · Cited by 49 · see citing works
Dubińska–Magiera, M., Zaremba-Czogalla, M., & Rzepecki, R. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1190-3 · Cited by 50 · see citing works
Tulgren, E. D., Turgeon, S. M., Opperman, K. J., & Grill, B. J. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004481 · Cited by 48 · see citing works
DNA repair deficiency and senescence in concussed professional athletes involved in contact sports
Schwab, N., Grenier, K., & Hazrati, L.-N. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0822-3 · Cited by 47 · see citing works
A‐type lamins and signaling: The PI 3‐kinase/Akt pathway moves forward
Marmiroli, S., Bertacchini, J., Beretti, F., Cenni, V., Guida, M., Pol, A. D., Maraldi, N. M., & Lattanzi, G. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21807 · Cited by 46 · see citing works
Azibani, F., Muchir, A., Vignier, N., Bonne, G., & Bertrand, A. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.01.001 · Cited by 45 · see citing works
The Biology of the Nuclear Envelope and Its Implications in Cancer Biology
Alvarado-Kristensson, M., & Rosselló, C. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102586 · Cited by 43 · see citing works
Lamin Mutations Cause Increased YAP Nuclear Entry in Muscle Stem Cells
Owens, D. J., Fischer, M., Jabre, S., Moog, S., Mamchaoui, K., Butler-Browne, G. S., & Coirault, C. (2020) · Cells · doi:10.3390/cells9040816 · Cited by 44 · see citing works
Loss of Emerin Alters Myogenic Signaling and miRNA Expression in Mouse Myogenic Progenitors
Koch, A. J., & Holaska, J. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037262 · Cited by 43 · see citing works
From structural resilience to cell specification — Intermediate filaments as regulators of cell fate
Sjöqvist, M., Antfolk, D., Rodriguez, F. S., & Sahlgren, C. (2020) · The FASEB Journal · doi:10.1096/fj.202001627r · Cited by 42 · see citing works
Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins
Gómez-Cavazos, J. S., & Hetzer, M. W. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.08.008 · Cited by 42 · see citing works
Functions of the nuclear envelope and lamina in development and disease
Cohen, T. V., Hernandez, L. F., & Stewart, C. L. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361329 · Cited by 42 · see citing works
Berk, J. M., Maitra, S., Dawdy, A., Shabanowitz, J., Hunt, D. F., & Wilson, K. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.503060 · Cited by 41 · see citing works
Barkan, R., Zahand, A. J., Sharabi, K., Lamm, A. T., Feinstein, N., Haithcock, E., Wilson, K. L., Liu, J., & Gruenbaum, Y. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-06-0505 · Cited by 41 · see citing works
Messages from the voices within: regulation of signaling by proteins of the nuclear lamina
Gerace, L., & Tapia, O. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.12.009 · Cited by 41 · see citing works
The Role of Emerin in Cancer Progression and Metastasis
Liddane, A. G., & Holaska, J. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011289 · Cited by 39 · see citing works
Molecular Regulators of Cellular Mechanoadaptation at Cell–Material Interfaces
Jo, J., Nansa, S. A., & Kim, D. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.608569 · Cited by 39 · see citing works
The Pathogenesis and Therapies of Striated Muscle Laminopathies
Brull, A., Rodríguez, B. M., Bonne, G., Muchir, A., & Bertrand, A. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01533 · Cited by 39 · see citing works
Tissue-Specific Defects Are Caused by Loss of the Drosophila MAN1 LEM Domain Protein
Pinto, B. S., Wilmington, S. R., Hornick, E. E., Wallrath, L. L., & Geyer, P. (2008) · Genetics · doi:10.1534/genetics.108.091371 · Cited by 39 · see citing works
- 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