Identification and Functional Analysis of Tomato BRI1 and BAK1 Receptor Kinase Phosphorylation Sites1[W][OPEN]

نویسندگان

  • Vikramjit S. Bajwa
  • Xiaofeng Wang
  • R. Kevin Blackburn
  • Michael B. Goshe
  • Srijeet K. Mitra
  • Elisabeth L. Williams
  • Gerard J. Bishop
  • Sergei Krasnyanski
  • George Allen
  • Steven C. Huber
  • Steven D. Clouse
چکیده

Department of Horticultural Science (V.S.B., X.W., S.K.M., S.K., G.A., S.D.C.) and Department of Molecular and Structural Biochemistry (R.K.B., M.B.G.), North Carolina State University, Raleigh, North Carolina 27695; Plant and Crop Sciences, University of Nottingham, Nottingham NG7 2RD, United Kingdom (E.L.W.); East Malling Research, East Malling, Kent ME19 6BJ, United Kingdom (G.J.B.); and United States Department of Agriculture/Agricultural Research Service, University of Illinois, Urbana, Illinois 61801 (S.C.H.)

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Identification and functional analysis of tomato BRI1 and BAK1 receptor kinase phosphorylation sites.

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The plasma membrane-localized BRI1-ASSOCIATED KINASE1 (BAK1) functions as a co-receptor with several receptor kinases including the brassinosteroid (BR) receptor BRASSINOSTEROID-INSENSITIVE 1 (BRI1), which is involved in growth, and the receptors for bacterial flagellin and EF-Tu, FLAGELLIN-SENSING 2 (FLS2) and EF-TU RECEPTOR (EFR), respectively, which are involved in immunity. BAK1 is a dual s...

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BRI1/BAK1, a Receptor Kinase Pair Mediating Brassinosteroid Signaling

The Arabidopsis BAK1 (BRI1 Associated receptor Kinase 1) was identified by a yeast two-hybrid screen as a specific interactor for BRI1, a critical component of a membrane brassinosteroid (BR) receptor. In yeast, BAK1/BRI1 interaction activates their kinase activities through transphosphorylation. BAK1 and BRI1 share similar gene expression and subcellular localization patterns and physically as...

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تاریخ انتشار 2013