Dystroglycan interacts with multiple partners, including the transmembrane receptor Celsr3, to regulate axon tract formation throughout the developing nervous system.

Neuronal interacting proteome reveals that the cellular dynamics of the lissencephaly-associated extracellular matrix receptor dystroglycan are governed by the exocyst complex, which is key for proper brain assembly.

Loss of functional dystroglycan disrupts the formation and function of CCK⁺/CB₁R⁺ inhibitory synapses in hippocampal CA1, resulting in reduced seizure thresholds in mouse models of dystroglycanopathy.

A Notch-mediated signaling pathway upregulates a Sec14-GOLD phosphopholipid binding protein that promotes a morphogenetic process important in tissue remodeling and renewal.

The correct enzymatic activity of a previously misnamed enzyme is defined, placing the enzyme upstream of LARGE in building functional O-mannose structures on α-dystroglycan that are disrupted in multiple forms of congenital muscular dystrophy.

Post-phosphoryl modification of α-dystroglycan requires the glucuronyltransferase B4GAT1; this enzyme synthesizes the acceptor glycan that serves as a primer for the glycosyltransferase LARGE to synthesize the laminin-binding glycan.

The combined use of NAD+ with ribitol or ribose potentiates the rescue of α-dystroglycan functional glycosylation in FKRP-mutant patient-specific iPSC-derived myotubes, representing potential novel treatments for FKRP muscular dystrophies.

N-terminal domain of dystroglycan enables like-acetylglucosaminyl transferase to elongate matriglycan on α-dystroglycan and prevent skeletal muscle pathophysiology.

InSyn1 is a new inhibitory post-synaptic protein that is essential for the dystroglycan complex, neuronal activity in vitro and in vivo, and cognitive behavior.

Protein O-Mannose Kinase enables Like-acetyl-glucosaminyltransferase 1 to elongate matriglycan on α-dystroglycan, thereby allowing matriglycan to function as a scaffold for extracellular matrix proteins and prevent muscular dystrophy.