Nathanael A Caveney, Naotaka Tsutsumi, K Christopher Garcia
Cryo-EM structures reveal GC-C associates with regulatory heat shock proteins similarly to bona fide protein kinases and this can guide the further development of mGC-targeted therapeutics.
Mammalian cells were engineered to synthesize valine, a metabolic capacity that had been lost from the lineage of higher eukaryotes for >500 million years.
Attaching a molecule of adenosine mono-phosphate (AMP) to the BiP protein at threonine 518 regulates its chaperone activity in the endoplasmic reticulum.
Biophysical and functional data strongly support the notion that Munc18-1 acts as a template to assemble the neuronal SNARE complex, and that inhibition of this activity underlies diverse forms of regulation of neurotransmitter release.
AMPylation of BiP allosterically interferes with stimulation of its ATPase activity by J-proteins that is required for high affinity substrate binding.
Cryo-electron tomography, reconstitution, and electrophysiological data show that a fundamental function of Munc13-1 is to bridge synaptic vesicles to the presynaptic plasma membrane.