Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry

Stephen J. Juris, Kavita Shah, Kevan Shokat, Jack E. Dixon, Panayiotis O. Vacratsis

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

Yersinia encodes a protein kinase, YpkA, which disrupts the actin cytoskeleton. Using an approach termed chemical genetics, we identified a 36-kDa substrate for YpkA in both J774 lysates and bovine brain cytosol. Mass spectrometry analysis identified this substrate as FLJ20113, an open reading frame that corresponds to otubain 1, a deubiquitinating enzyme implicated in immune cell clonal anergy. We demonstrate that otubain 1 is phosphorylated by YpkA in vitro and interacts with YpkA and actin in vivo. Identification of otubain 1 as a YpkA substrate suggests that regulation of immune cell anergy may be a survival mechanism for Yersinia.

Original languageEnglish
Pages (from-to)179-183
Number of pages5
JournalFEBS Letters
Volume580
Issue number1
DOIs
StatePublished - Jan 9 2006

Keywords

  • Chemical genetics
  • Phosphorylation
  • Protein kinase
  • Yersinia pathogenesis

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