
How LINC complexes mediate nuclear mechanotransduction remains unclear. In this issue, Déjardin, Carollo, et al. (2020. J. Cell Biol.https://doi.org/10.1083/jcb.201908036) show that the LINC complex protein nesprin-2G is a mechanosensor of epithelial–mesenchymal transitions (EMTs), recruiting α-catenin to the nucleus to attenuate Wnt/β-catenin signaling.
Cell Nucleus, 570, Biomedical and clinical sciences, Epithelial-Mesenchymal Transition, Mechanotransduction, 1.1 Normal biological development and functioning, 610, Nuclear Proteins, Biological Sciences, Medical and Health Sciences, Mechanotransduction, Cellular, Biological sciences, 2.1 Biological and endogenous factors, Biochemistry and Cell Biology, Generic health relevance, Cellular, Spotlight, beta Catenin, Developmental Biology
Cell Nucleus, 570, Biomedical and clinical sciences, Epithelial-Mesenchymal Transition, Mechanotransduction, 1.1 Normal biological development and functioning, 610, Nuclear Proteins, Biological Sciences, Medical and Health Sciences, Mechanotransduction, Cellular, Biological sciences, 2.1 Biological and endogenous factors, Biochemistry and Cell Biology, Generic health relevance, Cellular, Spotlight, beta Catenin, Developmental Biology
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 4 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 10% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Average | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |
