[HTML][HTML] Structure and intermolecular interactions of the luminal dimerization domain of human IRE1α
CY Liu, Z Xu, RJ Kaufman - Journal of Biological Chemistry, 2003 - ASBMB
Accumulation of unfolded proteins in the lumen of the endoplasmic reticulum activates a
signal transduction cascade that culminates in the transcriptional induction of genes
encoding adaptive functions. One proximal sensor for this unfolded protein response is the
protein kinase/endoribonuclease IRE1α. IRE1α is a type-I transmembrane glycoprotein for
which the N-terminal luminal domain (NLD) senses the accumulation of unfolded proteins.
Previously we demonstrated that the NLD forms a stable ligand-independent dimer linked by …
signal transduction cascade that culminates in the transcriptional induction of genes
encoding adaptive functions. One proximal sensor for this unfolded protein response is the
protein kinase/endoribonuclease IRE1α. IRE1α is a type-I transmembrane glycoprotein for
which the N-terminal luminal domain (NLD) senses the accumulation of unfolded proteins.
Previously we demonstrated that the NLD forms a stable ligand-independent dimer linked by …