論文

査読有り
2008年12月

Molecular basis of actin reorganization promoted by binding of enterohaemorrhagic Escherichia coli EspB to alpha-catenin

FEBS JOURNAL
  • Mitsuhide Hamaguchi
  • ,
  • Daizo Hamada
  • ,
  • Kayo N. Suzuki
  • ,
  • Ikuhiro Sakata
  • ,
  • Itaru Yanagihara

275
24
開始ページ
6260
終了ページ
6267
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1111/j.1742-4658.2008.06750.x
出版者・発行元
WILEY-BLACKWELL

EspB is a multifunctional protein associated with the type III secretion system of enterohaemorrhagic Escherichia coli, and interacts with various biomolecules including alpha-catenin in the host cell. The binding of EspB to alpha-catenin is thought be involved in actin reorganization during bacterial infection, although the precise mechanism of this phenomenon is still unclear. Recent research shows that dimerization of alpha-catenin dissociates it from E-cadherin/beta-catenin/alpha-catenin complexes, and that the dimer suppresses Arp2/3-mediated actin branching or polymerization. These results inspired us to evaluate the effect of EspB on the functions of alpha-catenin. Based on a series of in vitro biochemical approaches, including pull-down, co-sedimentation and pyrene-actin polymerization assays combined with transmission electron microscopy, we conclude that EspB promotes all the functions of dimeric alpha-catenin described above. These results clarified the molecular basis of reorganization of actin filaments during infection with enterohaemorrhagic Escherichia coli.

Web of Science ® 被引用回数 : 8

リンク情報
DOI
https://doi.org/10.1111/j.1742-4658.2008.06750.x
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/19016843
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000261184700021&DestApp=WOS_CPL

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