Journal
JOURNAL OF CELL BIOLOGY
Volume 177, Issue 4, Pages 613-624Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200611063
Keywords
-
Categories
Funding
- NIAID NIH HHS [AI19687, AI60723, R01 AI060723, R01 AI019687] Funding Source: Medline
Ask authors/readers for more resources
The mechanism by which substrates for endoplasmic reticulum-associated degradation are retrotranslocated to the cytosol remains largely unknown, although ubiquitination is known to play a key role. The mouse gamma-herpesvirus protein mK3 is a viral RING-CH-type E3 ligase that specifically targets nascent major histocompatibility complex I heavy chain (HC) for degradation, thus blocking the immune detection of virus-infected cells. To address the question of how HC is retrotranslocated and what role mK3 ligase plays in this action, we investigated ubiquitin conjugation sites on HC using mutagenesis and biochemistry approaches. In total, our data demonstrate that mK3-mediated ubiquitination can occur via serine, threonine, or lysine residues on the HC tail, each of which is sufficient to induce the rapid degradation of HC. Given that mK3 has numerous cellular and viral homologues, it will be of considerable interest to determine the pervasiveness of this novel mechanism of ubiquitination.
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