Abstract
Nicotinamide adenine dinucleotide (NAD+) participates in intracellular and extracellular signaling events unrelated to metabolism. In animals, purinergic receptors are required for extracellular NAD+ (eNAD+) to evoke biological responses, indicating that eNAD+ may be sensed by cell-surface receptors. However, the identity of eNAD+-binding receptors still remains elusive. Here, we identify a lectin receptor kinase (LecRK), LecRK-I.8, as a potential eNAD+ receptor in Arabidopsis. The extracellular lectin domain of LecRK-I.8 binds NAD+ with a dissociation constant of 436.5 ± 104.8 nM, although much higher concentrations are needed to trigger in vivo responses. Mutations in LecRK-I.8 inhibit NAD+-induced immune responses, whereas overexpression of LecRK-I.8 enhances the Arabidopsis response to NAD+. Furthermore, LecRK-I.8 is required for basal resistance against bacterial pathogens, substantiating a role for eNAD+ in plant immunity. Our results demonstrate that lectin receptors can potentially function as eNAD+-binding receptors and provide direct evidence for eNAD+ being an endogenous signaling molecule in plants.
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Claims 7
Claim · model-written summary
LecRK-I.8 was identified as a potential extracellular NAD+ receptor in Arabidopsis.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianat0 - Gene
- LecRK-I.8e0
- Compound
- eNAD+e0
- Outcome
- potential eNAD+ receptore0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e0“we identify a lectin receptor kinase (LecRK), LecRK-I.8, as a potential eNAD+ receptor in Arabidopsis.”
Claim · model-written summary
The LecRK-I.8 extracellular lectin domain bound NAD+ with a dissociation constant of 436.5 ± 104.8 nM.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Gene
- LecRK-I.8e0
- Compound
- NAD+e0
- Outcome
- binds NAD+e0
- Value
- 436.5 ± 104.8 nMe0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e0“The extracellular lectin domain of LecRK-I.8 binds NAD+ with a dissociation constant of 436.5 ± 104.8 nM”
Claim · model-written summary
In vivo responses required much higher NAD+ concentrations than binding.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Outcome
- in vivo responsese0
- Direction
- much highere0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e0“although much higher concentrations are needed to trigger in vivo responses.”
Claim · model-written summary
LecRK-I.8 mutations inhibited NAD+-induced immune responses.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Treatment
- Mutations in LecRK-I.8e0
- Gene
- LecRK-I.8e0
- Outcome
- NAD+-induced immune responsese0
- Direction
- inhibite0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e0“Mutations in LecRK-I.8 inhibit NAD+-induced immune responses”
Claim · model-written summary
LecRK-I.8 overexpression enhanced Arabidopsis response to NAD+.
- Taxon
- ArabidopsisArabidopsise0
- Treatment
- overexpression of LecRK-I.8e0
- Gene
- LecRK-I.8e0
- Outcome
- Arabidopsis response to NAD+e0
- Direction
- enhancese0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“overexpression of LecRK-I.8 enhances the Arabidopsis response to NAD+”
Claim · model-written summary
LecRK-I.8 was required for basal resistance to bacterial pathogens.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Interactor
- bacterial pathogense0pathogen
- Gene
- LecRK-I.8e0
- Outcome
- basal resistance against bacterial pathogense0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e0“LecRK-I.8 is required for basal resistance against bacterial pathogens”
Claim · model-written summary
The authors interpret eNAD+ as an endogenous signaling molecule in plants.
- Taxon
- plantsViridiplantaee0
- Compound
- eNAD+e0
- Outcome
- endogenous signaling moleculee0
Verbatim
e0“provide direct evidence for eNAD+ being an endogenous signaling molecule in plants.”
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