Ontology highlight
ABSTRACT:
SUBMITTER: Seidler PM
PROVIDER: S-EPMC4188734 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
Seidler Paul M PM Shinsky Stephen A SA Hong Feng F Li Zihai Z Cosgrove Michael S MS Gewirth Daniel T DT
Journal of molecular biology 20140903 21
Grp94 is a macromolecular chaperone belonging to the hsp90 family and is the most abundant glycoprotein in the endoplasmic reticulum (ER) of mammals. In addition to its essential role in protein folding, Grp94 was proposed to participate in the ER-associated degradation quality control pathway by interacting with the lectin OS-9, a sensor for terminally misfolded proteins. To understand how OS-9 interacts with ER chaperone proteins, we mapped its interaction with Grp94. Glycosylation of the full ...[more]