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Published 24 December 2001. doi:10.1083/jcb.200111010
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© The Rockefeller University Press, 0021-9525/2001/12/1265 $5.00
The Journal of Cell Biology, Volume 155, Number 7, December 24, 2001 1265-1274

Article

 A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition

Laurent Coscoy, David Jesse Sanchez and Don Ganem

Howard Hughes Medical Institute and Department of Microbiology, University of California Medical Center, San Francisco, CA 94143

Address correspondence to Don Ganem, Howard Hughes Medical Institute, Dept. of Microbiology, San Francisco, CA 94143. Tel.: (415) 476-2826. Fax: (415) 476-0939. E-mail: ganem{at}cgl.ucsf.edu

Kaposi's sarcoma-associated herpesvirus encodes two transmembrane proteins (modulator of immune recognition [MIR]1 and MIR2) that downregulate cell surface molecules (MHC-I, B7.2, and ICAM-1) involved in the immune recognition of infected cells. This downregulation results from enhanced endocytosis and subsequent endolysosomal degradation of the target proteins. Here, we show that expression of MIR1 and MIR2 leads to ubiquitination of the cytosolic tail of their target proteins and that ubiquitination is essential for their removal from the cell surface. MIR1 and MIR2 both contain cytosolic zinc fingers of the PHD subfamily, and these structures are required for this activity. In vitro, addition of a MIR2–glutathione S-transferase (GST) fusion protein to purified E1 and E2 enzymes leads to transfer of ubiquitin (Ub) to GST-containing targets in an ATP- and E2-dependent fashion; this reaction is abolished by mutation of the Zn-coordinating residues of the PHD domain. Thus, MIR2 defines a novel class of membrane-bound E3 Ub ligases that modulates the trafficking of host cell membrane proteins.

Key Words: herpesvirus; KSHV; ubiquitin; endocytosis; immunity


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