Membralin mutant mice manifest a severe and early-onset motor neuron disease with defects in endoplasmic reticulum-associated protein degradation.

When non-glycosylated, Seipin, which spans the endoplasmic reticulum (ER) membrane twice, forms aggregates in an oligomerization-dependent manner, distorts the shape of the ER, and incorporates SERCA2b via direct interaction, inactivation of which results in induction of ER stress and apoptosis.

A dual role of immune cells was found in ALS prognosis, where neutrophils and monocytes primarily reflect functional status whereas NK cells and different T lymphocyte populations act as prognostic markers for survival.

An agonist antibody to MuSK, delivered after disease onset, decreases the loss of neuromuscular synapses, improves motor function and extends the lifespan of ALS mice.

A mutagenesis screen in budding yeast sheds light on dynein regulation and function, and reveals the molecular basis for disease in patients suffering from neuropathies caused by dynein dysfunction.

Glutamate excitotoxicity induces a circuit-dependent ROS feedback loop to alter motor system integrity.

Proteins of the reticulon and REEP families, homologous to the products of human Hereditary Spastic Paraplegia disease genes, contribute to shaping and continuity of the axonal endoplasmic reticulum network in Drosophila.

In the SOD1^G93A mouse model of amyotrophic lateral sclerosis (ALS), expression of transmembrane signaling molecule ephrinB2 in spinal cord astrocytes contributes to motor neuron damage and loss of diaphragm function.

Elevating FUS level by saturating autoregulation loop in mice causes aggressive motor neuron disease via disrupting protein and RNA homeostasis.

The C9orf72 expansion binds and sequesters the splicing factor hnRNP H leading to insoluble G-quadruplex aggregates that functionally reduce hnRNP H, thereby producing splicing defects.