The geminivirus nuclear shuttle protein is a virulence factor that suppresses transmembrane receptor kinase activity

  1. Elizabeth P.B. Fontes1,3,
  2. Anesia A. Santos1,
  3. Dirce F. Luz1,
  4. Alessandro J. Waclawovsky1, and
  5. Joanne Chory2
  1. 1Departamento de Bioquímica e Biologia Molecular/BIOGRO/UFV, 36571.000, Viçosa, MG, Brazil; 2Howard Hughes Medical Institute and Plant Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037, USA

Abstract

Despite the large number of leucine-rich-repeat (LRR) receptor-like-kinases (RLKs) in plants and their conceptual relevance in signaling events, functional information is restricted to a few family members. Here we describe the characterization of new LRR-RLK family members as virulence targets of the geminivirus nuclear shuttle protein (NSP). NSP interacts specifically with three LRR-RLKs, NIK1, NIK2, and NIK3, through an 80-amino acid region that encompasses the kinase active site and A-loop. We demonstrate that these NSP-interacting kinases (NIKs) are membrane-localized proteins with biochemical properties of signaling receptors. They behave as authentic kinase proteins that undergo autophosphorylation and can also phosphorylate exogenous substrates. Autophosphorylation occurs via an intermolecular event and oligomerization precedes the activation of the kinase. Binding of NSP to NIK inhibits its kinase activity in vitro, suggesting that NIK is involved in antiviral defense response. In support of this, infectivity assays showed a positive correlation between infection rate and loss of NIK1 and NIK3 function. Our data are consistent with a model in which NSP acts as a virulence factor to suppress NIK-mediated antiviral responses.

Keywords

Footnotes

  • Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1245904.

  • 3 Corresponding author. E-MAIL bbfontes{at}ufv.br; FAX 55-31-3899-2864.

    • Accepted August 23, 2004.
    • Received August 3, 2004.
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