GnT1IP-L is a membrane bound glycoprotein that interacts with MGAT1 in the Golgi, but not in the endoplasmic reticulum, to regulate complex N-glycan synthesis.
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 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.
A multi-scale integration of experimental and computational approaches shows how a non-linear dependence of T-type calcium channel gating on GABAB receptor activity regulates thalamic network oscillations.
Metabolic switches between oxidative phosphorylation and aerobic glycolysis plus glutaminolysis direct T cell function by altering the flux of glucose and glutamine to N-glycosylation.