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

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 t...

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Bibliographic Details
Published in:Genes & development 2004-10, Vol.18 (20), p.2545-2556
Main Authors: Fontes, Elizabeth P B, Santos, Anesia A, Luz, Dirce F, Waclawovsky, Alessandro J, Chory, Joanne
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Arabidopsis - virology
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Binding Sites
Geminiviridae - metabolism
Geminiviridae - pathogenicity
Geminivirus
Membrane Proteins - metabolism
Microscopy, Fluorescence
Molecular Sequence Data
Phosphorylation
Protein Binding
Protein Kinases - metabolism
Recombinant Fusion Proteins
Research Papers
Reverse Transcriptase Polymerase Chain Reaction
Sequence Alignment
Sequence Analysis, DNA
Signal Transduction
Two-Hybrid System Techniques
Viral Proteins - genetics
Viral Proteins - metabolism
Virulence - genetics
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Summary: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.
ISSN:0890-9369
1549-5477
DOI:10.1101/gad.1245904