Journal
CELL
Volume 152, Issue 5, Pages 1184-1194Publisher
CELL PRESS
DOI: 10.1016/j.cell.2013.01.037
Keywords
-
Categories
Funding
- National Institute of General Medical Sciences [5R01 GM51923]
- ALS Association [K2Y740]
- Fidelity Biosciences Research Initiative
- German Research Foundation [GR 1517/12-1]
- Swiss Multiple Sclerosis Society
- Swiss National Science Foundation [31003A_138451]
- Medical Research Council
- MRC [G0802822] Funding Source: UKRI
- Swiss National Science Foundation (SNF) [31003A_138451] Funding Source: Swiss National Science Foundation (SNF)
- Medical Research Council [G0802822] Funding Source: researchfish
Ask authors/readers for more resources
Immunoproteasomes are alternative forms of proteasomes that have an enhanced ability to generate antigenic peptides. Recently, Seifert and colleagues reported surprising observations concerning the functions of immunoproteasomes and cellular responses to interferon-gamma: (1) that immunoproteasomes degrade ubiquitinated proteins faster than the constitutive proteasomes, (2) that polyubiquitin conjugates accumulate after interferon-gamma treatment but then are preferentially degraded by immunoproteasomes, and (3) that immunoproteasome deficiency causes the formation of inclusions and more severe experimental autoimmune encephalomyelitis (EAE). In contrast, we find that polyubiquitin conjugates do not transiently accumulate following IFN gamma-treatment and that immunoproteasomes do not prevent the formation of intracellular inclusions or protect against EAE. Furthermore, purified 26S constitutive and immunoproteasomes bind ubiquitin conjugates similarly and degrade them at similar rates. We conclude that, although immunoproteasomes can increase the generation of peptides appropriate for MHC class I presentation, they do not degrade ubiquitinated proteins more efficiently than constitutive particles.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available