Yersinia effector YopO uses actin as bait to phosphorylate proteins that regulate actin polymerization

Wei Lin Lee, Jonathan M. Grimes, Robert C. Robinson

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Pathogenic Yersinia species evade host immune systems through the injection of Yersinia outer proteins (Yops) into phagocytic cells. One Yop, YopO, also known as YpkA, induces actin-filament disruption, impairing phagocytosis. Here we describe the X-ray structure of Yersinia enterocolitica YopO in complex with actin, which reveals that YopO binds to an actin monomer in a manner that blocks polymerization yet allows the bound actin to interact with host actin-regulating proteins. SILAC-MS and biochemical analyses confirm that actin-polymerization regulators such as VASP, EVL, WASP, gelsolin and the formin diaphanous 1 are directly sequestered and phosphorylated by YopO through formation of ternary complexes with actin. This leads to a model in which YopO at the membrane sequesters actin from polymerization while using the bound actin as bait to recruit, phosphorylate and misregulate host actin-regulating proteins to disrupt phagocytosis.

Original languageEnglish
Pages (from-to)248-255
Number of pages8
JournalNature Structural and Molecular Biology
Volume22
Issue number3
DOIs
Publication statusPublished - Mar 6 2015
Externally publishedYes

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ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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