Paper · 2007 · The Plant Cell

Physical Association of the NB-LRR Resistance Protein Rx with a Ran GTPase–Activating Protein Is Required for Extreme Resistance toPotato virus X

Wladimir I.L. Tameling; David C. Baulcombe

6
claims
13
verbatim quotes
195
citations
2
research areas
✓
Open access · cc-by-nc

Abstract

Nucleotide binding leucine-rich repeat (NB-LRR) proteins play an important role in plant and mammalian innate immunity. In plants, these resistance proteins recognize specific pathogen-derived effector proteins. Recognition subsequently triggers a rapid and efficient defense response often associated with the hypersensitive response and other poorly understood processes that suppress the pathogen. To investigate mechanisms associated with the activation of disease resistance responses, we investigated proteins binding to the potato (Solanum tuberosum) NB-LRR protein Rx that confers extreme resistance to Potato virus X (PVX) in potato and Nicotiana benthamiana. By affinity purification experiments, we identified an endogenous N. benthamiana Ran GTPase-Activating Protein2 (RanGAP2) as an Rx-associated protein in vivo. Further characterization confirmed the specificity of this interaction and showed that the association occurs through their N-terminal domains. By specific virus-induced gene silencing of RanGAP2 in N. benthamiana carrying Rx, we demonstrated that this interaction is required for extreme resistance to PVX and suggest that RanGAP2 is part of the Rx signaling complex. These results implicate RanGAP-mediated cellular mechanisms, including nucleocytoplasmic trafficking, in the activation of disease resistance.

Abstract from the paper’s OpenAlex record; open copy licensed cc-by-nc. Read at the source ↗

The text the model read, with the source record’s inline markup (italics, sub- and superscripts) rendered and its character entities decoded; quote offsets refer to the raw text.

Claims 6

Observationobservedoriginal resultmeasured

Claim · model-written summary

N. benthamiana RanGAP2 was identified as an Rx-associated protein in vivo.

Taxon
N. benthamianaNicotiana benthamianae0
Gene
Ran GTPase-Activating Protein2 (RanGAP2)e0
Outcome
Rx-associated protein in vivoe0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“we identified an endogenous N. benthamiana Ran GTPase-Activating Protein2 (RanGAP2) as an Rx-associated protein in vivo”

✓ located verbatim in the source · abstract, characters 707–826 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

The RanGAP2–Rx interaction was specific.

Taxon
N. benthamianaNicotiana benthamianae2
Gene
RanGAP2e1
Outcome
specificity of this interactione0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“Further characterization confirmed the specificity of this interaction”

✓ located verbatim in the source · abstract, characters 828–898 · show in text ↑
e1

“Ran GTPase-Activating Protein2 (RanGAP2) as an Rx-associated protein”

✓ located verbatim in the source · abstract, characters 750–818 · show in text ↑
e2

“N. benthamiana Ran GTPase-Activating Protein2”

✓ located verbatim in the source · abstract, characters 735–780 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

Rx and RanGAP2 associated through their N-terminal domains.

Taxon
N. benthamianaNicotiana benthamianae2
Gene
RanGAP2e1
Outcome
association occurs through their N-terminal domainse0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“the association occurs through their N-terminal domains”

✓ located verbatim in the source · abstract, characters 915–970 · show in text ↑
e1

“Ran GTPase-Activating Protein2 (RanGAP2) as an Rx-associated protein”

✓ located verbatim in the source · abstract, characters 750–818 · show in text ↑
e2

“N. benthamiana Ran GTPase-Activating Protein2”

✓ located verbatim in the source · abstract, characters 735–780 · show in text ↑
Intervention effectobservedoriginal resultnegativemeasured

Claim · model-written summary

Silencing RanGAP2 in Rx-carrying N. benthamiana showed it is required for extreme resistance to PVX.

Taxon
N. benthamianaNicotiana benthamianae0
Treatment
virus-induced gene silencing of RanGAP2e0
Interactor
PVXPotato virus Xe0pathogen
Gene
RanGAP2e0
Outcome
extreme resistance to PVXe0

Not reportedComparatorDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“By specific virus-induced gene silencing of RanGAP2 in N. benthamiana carrying Rx, we demonstrated that this interaction is required for extreme resistance to PVX”

✓ located verbatim in the source · abstract, characters 972–1134 · show in text ↑
e1

“Potato virus X (PVX)”

✓ located verbatim in the source · abstract, characters 611–631 · show in text ↑
Mechanismauthor interpretationoriginal resultmeasured

Claim · model-written summary

The authors suggested RanGAP2 is part of the Rx signaling complex.

Taxon
N. benthamianaNicotiana benthamianae1
Gene
RanGAP2e0
Outcome
Rx signaling complexe0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“suggest that RanGAP2 is part of the Rx signaling complex”

✓ located verbatim in the source · abstract, characters 1139–1195 · show in text ↑
e1

“N. benthamiana carrying Rx”

✓ located verbatim in the source · abstract, characters 1027–1053 · show in text ↑
Mechanismauthor interpretationoriginal resultmeasured

Claim · model-written summary

The authors implicated RanGAP-mediated processes, including nucleocytoplasmic trafficking, in disease-resistance activation.

Taxon
N. benthamianaNicotiana benthamianae1
Outcome
activation of disease resistancee0
Qualifier
nucleocytoplasmic traffickinge0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Nicotiana benthamiana
Nicotiana benthamiana · TaxonCharles Andres · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

e0

“These results implicate RanGAP-mediated cellular mechanisms, including nucleocytoplasmic trafficking, in the activation of disease resistance”

✓ located verbatim in the source · abstract, characters 1197–1338 · show in text ↑
e1

“N. benthamiana carrying Rx”

✓ located verbatim in the source · abstract, characters 1027–1053 · show in text ↑

loss of function · Potato virus X · Nicotiana benthamianaPositive and negative results

15 papers: 8 positive, 7 negative or no effect

6 papers in the same direction as this paper · 8 in the opposite direction

  1. positive
  2. positive
  3. positive

11 papers more in this group

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Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.