ArticlePlant physiology2014
Plasma membrane localization is essential for Oryza sativa Pto-interacting protein 1a-mediated negative regulation of immune signaling in rice.
Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 33 citations in OpenAlex.
- RSLpred2: An Integrated Web Server for the Annotation of Rice Proteome Subcellular Localization Using Deep Learning.Rice (New York, N.Y.) · 2025Article
- AtSubP-2.0: An integrated web server for the annotation of Arabidopsis proteome subcellular localization using deep learning.The plant genome · 2025Article
- Article
- Advances in the Genetic Basis and Molecular Mechanism of Lesion Mimic Formation in Rice.Plants (Basel, Switzerland) · 2022Review
- Pto Interaction Proteins: Critical Regulators in Plant Development and Stress Response.Frontiers in plant science · 2022Review
- Genome-wide identification of PTI1 family in Setaria italica and salinity-responsive functional analysis of SiPTI1-5.BMC plant biology · 2021Article
- Identification of long noncoding RNAs involved in resistance to downy mildew in Chinese cabbage.Horticulture research · 2021Article
- Resistance to Sharka in Apricot: Comparison of Phase-Reconstructed Resistant and Susceptible Haplotypes of 'Lito' Chromosome 1 and Analysis of Candidate Genes.Frontiers in plant science · 2019Article
- Stable Accumulation of Photosystem II Requires ONE-HELIX PROTEIN1 (OHP1) of the Light Harvesting-Like Family.Plant physiology · 2018Article
- Rice immune regulator, OsPti1a, is specifically phosphorylated at the plasma membrane.Plant signaling & behavior · 2015Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oryza sativa Pto-interacting protein 1a (OsPti1a), an ortholog of tomato (Solanum lycopersicum) SlPti1, functions as a negative regulator of innate immunity in rice (Oryza sativa). In ospti1a mutants, the activation of immune responses, including hypersensitive response-like cell death, is caused by loss of the OsPti1a protein; however, it is as yet unclear how OsPti1a suppresses immune responses. Here, we report that OsPti1a localizes to detergent-resistant membrane fractions of the plasma membrane through lipid modification of the protein's amino terminus, which is highly conserved among Pti1 orthologs in several plant species. Importantly, mislocalization of OsPti1a after deletion of its amino terminus reduced its ability to complement the mutant phenotypes, including hypersensitive response-like cell death. Furthermore, complex formation of OsPti1a depends on its amino terminus-mediated membrane localization. Liquid chromatography-tandem mass spectrometry analysis of OsPti1a complex-interacting proteins identified several defense-related proteins. Collectively, these findings indicate that appropriate complex formation by OsPti1a at the plasma membrane is required for the negative regulation of plant immune responses in rice.
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