ArticlePlant signaling & behavior2018
Intramolecular crosstalk between catalytic activities of receptor kinases.
Article in Plant signaling & behavior, 2018. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Moonlighting Crypto-Enzymes and Domains as Ancient and Versatile Signaling Devices.International journal of molecular sciences · 2024Review
- Peptide-Mediated Cyclic Nucleotide Signaling in Plants: Identification and Characterization of Interactor Proteins with Nucleotide Cyclase Activity.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The discovery of hidden guanylate cyclases (GCs) in theComputational and structural biotechnology journal · 2023Article
- Moonlighting Proteins Shine New Light on Molecular Signaling Niches.International journal of molecular sciences · 2021Review
- Cross Talk Between Cyclic Nucleotides and Calcium Signaling Pathways in Plants-Achievements and Prospects.Frontiers in plant science · 2021Review
- Functional Crypto-Adenylate Cyclases Operate in Complex Plant Proteins.Frontiers in plant science · 2021Article
- New Perspectives on Plant Adenylyl Cyclases.Frontiers in molecular biosciences · 2019Article
- PlantMP: a database for moonlighting plant proteins.Database : the journal of biological databases and curation · 2019Article
- An Arabidopsis Clathrin Assembly Protein with a Predicted Role in Plant Defense Can Function as an Adenylate Cyclase.Biomolecules · 2018Article
- Downstream Targets of Cyclic Nucleotides in Plants.Frontiers in plant science · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Signal modulation is important for the growth and development of plants and this process is mediated by a number of factors including physiological growth regulators and their associated signal transduction pathways. Protein kinases play a central role in signaling, including those involving pathogen response mechanisms. We previously demonstrated an active guanylate cyclase (GC) catalytic center in the brassinosteroid insensitive receptor (AtBRI1) within an active intracellular kinase domain resulting in dual enzymatic activity. Here we propose a novel type of receptor architecture that is characterized by a functional GC catalytic center nested in the cytosolic kinase domain enabling intramolecular crosstalk. This may be through a cGMP-AtBRI1 complex forming that may induce a negative feedback mechanism leading to desensitisation of the receptor, regulated through the cGMP production pathway. We further argue that the comparatively low but highly localized cGMP generated by the GC in response to a ligand is sufficient to modulate the kinase activity. This type of receptor therefore provides a molecular switch that directly and/or indirectly affects ligand dependent phosphorylation of downstream signaling cascades and suggests that subsequent signal transduction and modulation works in conjunction with the kinase in downstream signaling.
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Registered trials
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.