ArticleProceedings of the National Academy of Sciences of the United States of America2007
Proteolysis of the barley receptor-like protein kinase RPG1 by a proteasome pathway is correlated with Rpg1-mediated stem rust resistance.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 42 citations in OpenAlex.
- Diverse epistatic effects in barley-powdery mildew interactions localize to host chromosome hotspots.iScience · 2024Article
- Characterization of Host-Specific Genes from Pine- and Grass-Associated Species of thePathogens (Basel, Switzerland) · 2022Article
- Mutations in a barley cytochrome P450 gene enhances pathogen induced programmed cell death and cutin layer instability.PLoS genetics · 2021Article
- Tandem Protein Kinases Emerge as New Regulators of Plant Immunity.Molecular plant-microbe interactions : MPMI · 2021Review
- A rare gain of function mutation in a wheat tandem kinase confers resistance to powdery mildew.Nature communications · 2020Article
- Transcriptome-wide association study identifies putative elicitors/suppressor of Puccinia graminis f. sp. tritici that modulate barley rpg4-mediated stem rust resistance.BMC genomics · 2019Article
- Characterization of genes required for both Rpg1 and rpg4-mediated wheat stem rust resistance in barley.BMC genomics · 2019Article
- Shedding Light on Penetration of Cereal Host Stomata by Wheat Stem Rust Using Improved Methodology.Scientific reports · 2019Article
- The early response during the interaction of fungal phytopathogen and host plant.Open biology · 2017Review
- Molecular and genetic characterization of barley mutants and genetic mapping of mutant rpr2 required for Rpg1-mediated resistance against stem rust.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2016Article
- The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice.PLoS pathogens · 2016Article
- Concerted action of two avirulent spore effectors activates Reaction to Puccinia graminis 1 (Rpg1)-mediated cereal stem rust resistance.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Parallel expression profiling of barley-stem rust interactions.Functional & integrative genomics · 2008Article
- Post-translational modification of host proteins in pathogen-triggered defence signalling in plants.Molecular plant pathology · 2008Review
- The wheat mitogen-activated protein kinases TaMPK3 and TaMPK6 are differentially regulated at multiple levels during compatible disease interactions with Mycosphaerella graminicola.Plant physiology · 2008Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In plants, disease resistance mediated by the gene-for-gene mechanism involves the recognition of specific effector molecules produced by the pathogen either directly or indirectly by the resistance-gene products. This recognition triggers a series of signals, thereby serving as a molecular switch in regulating defense mechanisms by the plants. To understand the mechanism of action of the barley stem rust resistance gene Rpg1, we investigated the fate of the RPG1 protein in response to infection with the stem rust fungus, Puccinia graminis f. sp. tritici. The investigations revealed that RPG1 disappears to undetectable limits only in the infected tissues in response to avirulent, but not virulent pathotypes. The RPG1 protein disappearance is rapid and appears to be due to specific protein degradation via the proteasome-mediated pathway as indicated by inhibition with the proteasomal inhibitor MG132, but not by other protease inhibitors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.