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Published online May 14, 2007
doi:10.1083/jcb.200611063
The Journal of Cell Biology, Vol. 177, No. 4, 613-624
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Wang et al.
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Article

 Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3

Xiaoli Wang1, Roger A. Herr1, Wei-Jen Chua1, Lonnie Lybarger2, Emmanuel J.H.J. Wiertz3, and Ted H. Hansen1

1 Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110
2 Department of Cell Biology and Anatomy, University of Arizona Health Sciences Center, Tucson, AZ 85724
3 Department of Medical Microbiology, Leiden University Medical Center, 2300 RC Leiden, Netherlands

Correspondence to Ted H. Hansen: hansen{at}pathology.wustl.edu

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.

Abbreviations used in this paper: 2ME, 2-mercaptoethanol; endo H, endoglycosidase H; ERAD, ER-associated degradation; HC, heavy chain; KSHV, Kaposi's sarcoma-associated herpesvirus; MHC, major histocompatibility complex; TAP, transporter associated with antigen processing; TMB, thrombin; Ub, ubiquitin; wt, wild type.


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