Calreticulin, beyond its known role as a chaperone, also serves as an endoplasmic reticulum repressor of ATF6⍺, selectively regulating one arm of the unfolded protein response.

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.

An essential role for ACAT in conferring 25HC-mediated protection against bacterial and viral infection has been uncovered.

Mammalian cells were engineered to synthesize valine, a metabolic capacity that had been lost from the lineage of higher eukaryotes for >500 million years.

Two different binding modes of the Munc13-1 C­₁C₂B region govern synaptic vesicle priming and neurotransmitter release probability.

Regulation of the endoplasmic reticulum chaperone BiP by calcium.

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.

AMPylation of BiP allosterically interferes with stimulation of its ATPase activity by J-proteins that is required for high affinity substrate binding.

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.

The notion that the drug-like small molecule Sephin1 protects against protein misfolding by selectively disrupting a cellular phosphatase is refuted.