Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins.

ABSTRACT: Stromal interaction molecule-1 (STIM1) is a type-I transmembrane protein located on the endoplasmic reticulum (ER) and plasma membranes (PM). ER-resident STIM1 regulates the activity of PM Orai1 channels in a process known as store operated calcium (Ca²⁺) entry which is the principal Ca²⁺ signaling process that drives the immune response. STIM1 undergoes post-translational N-glycosylation at two luminal Asn sites within the Ca²⁺ sensing domain of the molecule. However, the biochemical, biophysical, and structure biological effects of N-glycosylated STIM1 were poorly understood until recently due to an inability to readily obtain high levels of homogeneous N-glycosylated protein. Here, we describe the implementation of an in vitro chemical approach which att

SUBMITTER: Choi YJ 

PROVIDER: S-EPMC5752362 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature