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

doi:10.3390/ijms21175944

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Community

Back to search

Article

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

International journal of molecular sciences - 19 Aug 2020

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

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Active Transport, Cell Nucleus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to B-Lymphocytes

Share to Binding Sites

Share to Dystroglycans

Share to HeLa Cells

Share to Muscular Dystrophy, Emery-Dreifuss

Share to Nuclear Envelope

Share to Nuclear Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 32824881
DOI: 10.3390/ijms21175944
PMCID: PMC7504044

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Molecular Basis and Biologic Significance of the β-Dystroglycan-Emerin Interaction.PMID 32824881Read ↗

Emerin in health and disease.Semantic proximity Read ↗

Muscular Dystrophy Mutations Impair the Nuclear Envelope Emerin Self-assembly Properties.Semantic proximity Read ↗

Multiple and surprising new functions for emerin, a nuclear membrane protein.Semantic proximity Read ↗

The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane.Semantic proximity Read ↗

Distinct regions specify the nuclear membrane targeting of emerin, the responsible protein for Emery-Dreifuss muscular dystrophy.Semantic proximity Read ↗

Emerin self-assembly mechanism: role of the LEM domain.Semantic proximity Read ↗

A-type lamins anchor emerin at the inner nuclear membrane via two independent binding sitesSemantic proximity Read ↗

Emery-Dreifuss muscular dystrophy mutations impair TRC40-mediated targeting of emerin to the inner nuclear membrane.Semantic proximity Read ↗

Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery-Dreifuss muscular dystrophy.Semantic proximity Read ↗

Emery-Dreifuss muscular dystrophy at the nuclear envelope: 10 years on.Semantic proximity Read ↗

Emerin Represses STAT3 Signaling through Nuclear Membrane-Based Spatial ControlSemantic proximity Read ↗

Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.