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screen for isg15-crossreactive deubiquitinases屏幕isg15-crossreactive deubiquitinases
Screen for ISG15-crossreactive Deubiquitinases
´ 1,2.¤ 3. 2 ¨ 4 5 2
Andre Catic , Edda Fiebiger , Gregory A. Korbel , Daniel Blom , Paul J. Galardy *, Hidde L. Ploegh *
1 Program in Immunology, Harvard Medical School, Boston, Massachusetts, United States of America, 2 Whitehead Institute for Biomedical Research,
Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America, 3 GI Cell Biology, Children’s Hospital, Boston,
Massachusetts, United States of America, 4 Merck, Rahway, New Jersey, United States of America, 5 Mayo Clinic, Pediatric and Adolescent Medicine,
Rochester, Minnesota, United States of America
Background. The family of ubiquitin-like molecules (UbLs) comprises several members, each of which has sequence,
structural, or functional similarity to ubiquitin. ISG15 is a homolog of ubiquitin in vertebrates and is strongly upregulated
following induction by type I interferon. ISG15 can be covalently attached to proteins, analogous to ubiquitination and with
actual support of ubiquitin conjugating factors. Specific proteases are able to reverse modification with ubiquitin or UbLs by
hydrolyzing the covalent bond between their C-termini and substrate proteins. The tail regions of ubiquitin and ISG15 are
identical and we therefore hypothesized that promiscuous deubiquitinating proteases (DUBs) might exist, capable of
recognizing both ubiquitin and ISG15. Results. We have cloned and expressed 22 human DUBs, representing the major clades
of the USP protease family. Utilizing suicide inhibitors based on ubiquitin and ISG15, we have identified USP2, USP5 (IsoT1),
USP13 (IsoT3), and USP14 as ISG15-reactive proteases, in addition to the
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