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.
Department of Biochemistry and Molecular Biology, University of Massachusetts, 710N. Pleasant Street, Amherst, MA 01003, USA.
Taku
T
Tamura
James H
JH
Cormier
Daniel N
DN
Hebert
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