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

doi:10.1016/j.febslet.2005.11.071

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

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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 language	English
Pages (from-to)	179-183
Number of pages	5
Journal	FEBS Letters
Volume	580
Issue number	1
DOIs	https://doi.org/10.1016/j.febslet.2005.11.071
State	Published - Jan 9 2006

Keywords

Chemical genetics
Phosphorylation
Protein kinase
Yersinia pathogenesis

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

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.",

keywords = "Chemical genetics, Phosphorylation, Protein kinase, Yersinia pathogenesis",

author = "Juris, {Stephen J.} and Kavita Shah and Kevan Shokat and Dixon, {Jack E.} and Vacratsis, {Panayiotis O.}",

note = "Funding Information: This work was funded by National Institutes of Health (NIH) Grant 18849 (to J.E.D.), NIH Molecular Mechanisms of Microbial Pathogenesis Training Grant AI07528 (to S.J.J.), the Walther Cancer Institute (to J.E.D.), and the Ellison Foundation for Medical Research.",

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T1 - Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry

AU - Juris, Stephen J.

AU - Shah, Kavita

AU - Shokat, Kevan

AU - Dixon, Jack E.

AU - Vacratsis, Panayiotis O.

N1 - Funding Information: This work was funded by National Institutes of Health (NIH) Grant 18849 (to J.E.D.), NIH Molecular Mechanisms of Microbial Pathogenesis Training Grant AI07528 (to S.J.J.), the Walther Cancer Institute (to J.E.D.), and the Ellison Foundation for Medical Research.

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N2 - 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.

AB - 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.

KW - Chemical genetics

KW - Phosphorylation

KW - Protein kinase

KW - Yersinia pathogenesis

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JO - FEBS Letters

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

Abstract

Keywords

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