Journal article icon

Journal article

OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD.

Abstract:

Terminally misfolded or unassembled proteins in the early secretory pathway are degraded by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). How substrates of this pathway are recognized within the ER and delivered to the cytoplasmic ubiquitin-conjugating machinery is unknown. We report here that OS-9 and XTP3-B/Erlectin are ER-resident glycoproteins that bind to ERAD substrates and, through the SEL1L adaptor, to the ER-membrane-embedded ubiquitin ligas...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1038/ncb1689

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Ludwig Institute
Shaler, TA More by this author
Kopito, RR More by this author
Journal:
Nature cell biology
Volume:
10
Issue:
3
Pages:
272-282
Publication date:
2008-03-05
DOI:
EISSN:
1476-4679
ISSN:
1465-7392
URN:
uuid:a1a4abae-4dea-47ad-a8ea-8aecb988349b
Source identifiers:
53514
Local pid:
pubs:53514

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP