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Please click "PlantReports" above to follow us! Be the first to know the latest research progress in the field of plant science! Ma et al.
published a research paper titled "Membrane nanodomains modulate formin condensation for actin remodeling in Arabidopsis innate immune responses" in The Plant Cell online, revealing that plant cell membrane nanodomains condense formin proteins during pathogen infection Molecular mechanisms promoting actin remodeling in the innate immune response in Arabidopsis
.
Background review: When bacterial pathogens attack plants, the actin cytoskeleton in the plant host undergoes rapid remodeling to coordinate a series of host immune responses
.
Plasma membrane-localized formin proteins act as molecular switches for actin cytoskeleton polymerization in plant innate immune signal transduction pathways
.
We found in previous studies that bacterial-induced plant innate immunity induces macromolecular aggregation of formin proteins on the plant cell surface to form nanoscale molecular clusters, thereby activating the activity of formin proteins to act on actin polymerization
.
However, the underlying molecular mechanism by which pathogenic infection induces formin proteins to aggregate into nanoclusters on the cell surface remains unclear
.
Scientific question: We wanted to identify important biomolecules that drive the aggregation of formin proteins into nanoclusters on the cell surface and activate actin polymerization during pathogen infection
.
Because type I formin proteins on the plant cell surface differ from their GTPase-activated homologs in mammals, we explored other biophysical factors on the plant plasma membrane that can regulate the behavior of formin proteins and their effect on actin remodeling activity
.
Findings: We found that pathogenic infection caused the condensation of plant type I formin proteins, and that this process was dependent on the compartmentalization of the plasma membrane, i.
e.
the formation of nanodomains
.
Molecular aggregation of the nanodomain assembly protein remorin on the surface of plant cells is gradually enhanced during the early stages of pathogenic infection
.
We were surprised to find that the molecular aggregation of the actin nucleating protein formin and the nanodomain resident protein remorin on the cell surface exhibited a similar pattern of spatiotemporal regulation
.
Through quantitative studies of different methods, we finally resolved the interaction model of formin and remorin proteins on the cell membrane through artificial reorganization of lipid bilayers in vitro and in vivo cell biology imaging techniques
.
We further reconstructed the molecular pathway activated by actin remodeling, that is, remorin protein recruits, aggregates and activates formin protein through macromolecular condensation, thereby promoting actin multimerization
.
Looking to the future: We are working to enhance our overall understanding of some of the fundamental biological principles involved in how nanodomains on the surface of plant cells are assembled to activate or deactivate defense-related biomolecules, thereby enabling host-pathogen interactions in host-pathogen interactions.
The biochemical activity of these biomolecules is activated or deactivated during the course of action
.
This article is transferred from ThePlantCell official account, only for sharing and communication, without any commercial use
.
Click "Read the original text" in the lower left corner to view the full text of the paper
.
Long press the QR code below to follow Plant Reports! Follow the latest research progress in agricultural science and plant science! For investment and reprint, please contact plantreports@163.
com
published a research paper titled "Membrane nanodomains modulate formin condensation for actin remodeling in Arabidopsis innate immune responses" in The Plant Cell online, revealing that plant cell membrane nanodomains condense formin proteins during pathogen infection Molecular mechanisms promoting actin remodeling in the innate immune response in Arabidopsis
.
Background review: When bacterial pathogens attack plants, the actin cytoskeleton in the plant host undergoes rapid remodeling to coordinate a series of host immune responses
.
Plasma membrane-localized formin proteins act as molecular switches for actin cytoskeleton polymerization in plant innate immune signal transduction pathways
.
We found in previous studies that bacterial-induced plant innate immunity induces macromolecular aggregation of formin proteins on the plant cell surface to form nanoscale molecular clusters, thereby activating the activity of formin proteins to act on actin polymerization
.
However, the underlying molecular mechanism by which pathogenic infection induces formin proteins to aggregate into nanoclusters on the cell surface remains unclear
.
Scientific question: We wanted to identify important biomolecules that drive the aggregation of formin proteins into nanoclusters on the cell surface and activate actin polymerization during pathogen infection
.
Because type I formin proteins on the plant cell surface differ from their GTPase-activated homologs in mammals, we explored other biophysical factors on the plant plasma membrane that can regulate the behavior of formin proteins and their effect on actin remodeling activity
.
Findings: We found that pathogenic infection caused the condensation of plant type I formin proteins, and that this process was dependent on the compartmentalization of the plasma membrane, i.
e.
the formation of nanodomains
.
Molecular aggregation of the nanodomain assembly protein remorin on the surface of plant cells is gradually enhanced during the early stages of pathogenic infection
.
We were surprised to find that the molecular aggregation of the actin nucleating protein formin and the nanodomain resident protein remorin on the cell surface exhibited a similar pattern of spatiotemporal regulation
.
Through quantitative studies of different methods, we finally resolved the interaction model of formin and remorin proteins on the cell membrane through artificial reorganization of lipid bilayers in vitro and in vivo cell biology imaging techniques
.
We further reconstructed the molecular pathway activated by actin remodeling, that is, remorin protein recruits, aggregates and activates formin protein through macromolecular condensation, thereby promoting actin multimerization
.
Looking to the future: We are working to enhance our overall understanding of some of the fundamental biological principles involved in how nanodomains on the surface of plant cells are assembled to activate or deactivate defense-related biomolecules, thereby enabling host-pathogen interactions in host-pathogen interactions.
The biochemical activity of these biomolecules is activated or deactivated during the course of action
.
This article is transferred from ThePlantCell official account, only for sharing and communication, without any commercial use
.
Click "Read the original text" in the lower left corner to view the full text of the paper
.
Long press the QR code below to follow Plant Reports! Follow the latest research progress in agricultural science and plant science! For investment and reprint, please contact plantreports@163.
com
