- Abstract:
-
The mammalian ubiquitin ligase Hrd1 is the central component of a complex facilitating degradation of misfolded proteins during the ubiquitin-proteasome dependent process of ER-associated degradation (ERAD). Hrd1 associates with cofactors to execute ERAD, but their roles and how they assemble with Hrd1 are not well understood. Here we identify crucial cofactor interaction domains within Hrd1 and report a previously unrecognised evolutionarily conserved segment within the intrinsically disorde...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Accepted manuscript
- Files:
-
-
(pdf, 1.5mb)
-
(pdf, 155.3kb)
-
(pdf, 401.4kb)
-
- Publisher copy:
- 10.1242/jcs.206847
-
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- Publisher:
- Company of Biologists Publisher's website
- Journal:
- Journal of Cell Science Journal website
- Volume:
- 130
- Pages:
- 3322-3335
- Publication date:
- 2017-08-21
- Acceptance date:
- 2017-08-16
- DOI:
- EISSN:
-
1477-9137
- ISSN:
-
0021-9533
- Pubs id:
-
pubs:724220
- URN:
-
uri:bed8e119-d4b4-47ff-b737-d571ca6f5240
- UUID:
-
uuid:bed8e119-d4b4-47ff-b737-d571ca6f5240
- Local pid:
- pubs:724220
- Language:
- English
- Keywords:
- Copyright holder:
- Company of Biologists
- Copyright date:
- 2017
- Notes:
-
This is the accepted manuscript version of the article. The final version is
available online from Company of Biologists at: https://doi.org/10.1242/jcs.206847
Journal article
Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex formation for ER-associated degradation (ERAD)
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Ludwig Institute for Cancer Research
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