The Molecular Basis and Biological Significance of the β-Dystroglycan-Emerin Interaction

Wendy Lilián Gómez-Monsiváis , Feliciano Monterrubio-Ledezma, Jazmin Huerta-Cantillo, Ricardo Mondragon-Gonzalez, Alma Alamillo-Iniesta , Ian García-Aguirre , Paulina Margarita Azuara-Medina , Raúl Arguello-García , Jhon Erick Rivera-Monroy, ames M. Holaska, Jesús Mauricio Ernesto Hernández-Méndez , Efraín Garrido , Jonathan Javier Magaña *, Steve Winder, Andrea Brancaccio, Ivette Martínez-Vieyra , Fernando Navarro-Garcia , Bulmaro Cisneros*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

2 Citations (Scopus)
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β-dystroglycan (β-DG) assembles with lamins A/C and B1 and emerin at the nuclear envelope (NE) to maintain proper nuclear architecture and function. To provide insight into the nuclear function of β-DG, we characterized the interaction between β-DG and emerin at the molecular level. Emerin is a major NE protein that regulates multiple nuclear processes and whose deficiency results in Emery–Dreifuss muscular dystrophy (EDMD). Using truncated variants of β-DG and emerin, via a series of in vitro and in vivo binding experiments and a tailored computational analysis, we determined that the β-DG–emerin interaction is mediated at least in part by their respective transmembrane domains (TM). Using surface plasmon resonance assays we showed that emerin binds to β-DG with high affinity (KD in the nanomolar range). Remarkably, the analysis of cells in which DG was knocked out demonstrated that loss of β-DG resulted in a decreased emerin stability and impairment of emerin-mediated processes. β-DG and emerin are reciprocally required for their optimal targeting within the NE, as shown by immunofluorescence, western blotting and immunoprecipitation assays using emerin variants with mutations in the TM domain and B-lymphocytes of a patient with EDMD. In summary, we demonstrated that β-DG plays a role as an emerin interacting partner modulating its stability and function
Original languageEnglish
Article number5944
Number of pages21
JournalInternational Journal of Molecular Sciences
Issue number17
Publication statusPublished - 19 Aug 2020


  • β-dystroglycan
  • emerin
  • nuclear envelope
  • Emery-Dreifuss muscular dystrophy
  • surface plasmon resonance assay
  • proteasome


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