Sweet bays of ERAD.
Proteins that improperly mature in the endoplasmic reticulum (ER) are dislocated to the cytoplasm for proteasome-mediated destruction. A recent study provides insight into the incompletely understood processes for selection and targeting of aberrant proteins for ER-associated protein degradation. The identification of the ER chaperones GRP94 and BiP as binding partners for the mannose-binding proteins OS-9 and XTP3-B, indicates that these protein complexes bind to aberrant proteins and direct them to the Hrd1 dislocation and ubiquitylation complex in the ER membrane.
Tamura
Taku
T
Department of Biochemistry and Molecular Biology, University of Massachusetts, 710N. Pleasant Street, Amherst, MA 01003, USA.
Cormier
James H
JH
Hebert
Daniel N
DN
D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D037102:Lectins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D008954:Models, Biological; D009363:Neoplasm Proteins / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011485:Protein Binding
D037102:Lectins; D008565:Membrane Proteins; D009363:Neoplasm Proteins; C098898:OS9 protein, human; D046988:Proteasome Endopeptidase Complex