# The Role of β-Dystroglycan in Nuclear Dynamics

## TL;DR

This study investigates the role of β-dystroglycan in the nucleus, finding it affects nuclear size but not mechanical properties or stress resistance.

## Contribution

The study reveals a novel nuclear role for dystroglycan in regulating nuclear size.

## Key findings

- Dystroglycan is present in the nucleus of myoblast cells.
- Deleting dystroglycan changes nuclear size but not shape or stiffness.
- Reintroducing dystroglycan restores nuclear size in disrupted cells.

## Abstract

Dystroglycan is a ubiquitously expressed heterodimeric cell-surface laminin receptor with roles in cell adhesion, signalling, and membrane stabilisation. More recently, the transmembrane β-subunit of dystroglycan has been shown to localise to both the nuclear envelope and the nucleoplasm. This has led to the hypothesis that dystroglycan may have a structural role at the nuclear envelope analogous to its role at the plasma membrane. The biochemical fraction of myoblast cells clearly supports the presence of dystroglycan in the nucleus. Deletion of the dystroglycan protein by disruption of the DAG1 locus using CRISPR/Cas9 leads to changes in nuclear size but not overall morphology; moreover, the Young’s modulus of dystroglycan-deleted nuclei, as determined by atomic force microscopy, is unaltered. Dystroglycan-disrupted myoblasts are also no more susceptible to nuclear stresses including chemical and mechanical, than normal myoblasts. Re-expression of dystroglycan in DAG1-disrupted myoblasts restores nuclear size without affecting other nuclear parameters.