PAMP Signals in Plant Innate Immunity

Signal Perception and Transduction

Specificaties
Gebonden, 442 blz. | Engels
Springer Netherlands | 2014e druk, 2013
ISBN13: 9789400774254
Rubricering
Springer Netherlands 2014e druk, 2013 9789400774254
Verwachte levertijd ongeveer 9 werkdagen

Samenvatting

Plant innate immunity is a potential surveillance system of plants and is the first line of defense against invading pathogens. The immune system is a sleeping system in unstressed healthy plants and is activated on perception of the pathogen-associated molecular patterns (PAMP; the pathogen’s signature) of invading pathogens. The PAMP alarm/danger signals are perceived by plant pattern-recognition receptors (PRRs). The plant immune system uses several second messengers to encode information generated by the PAMPs and deliver the information downstream of PRRs to proteins which decode/interpret signals and initiate defense gene expression. This book describes the most fascinating PAMP-PRR signaling complex and signal transduction systems. It also discusses the highly complex networks of signaling pathways involved in transmission of the signals to induce distinctly different defense-related genes to mount offence against pathogens.

Specificaties

ISBN13:9789400774254
Taal:Engels
Bindwijze:gebonden
Aantal pagina's:442
Uitgever:Springer Netherlands
Druk:2014

Inhoudsopgave

<p>1. Introduction<br>1.1Classical PAMPs<br> 1.2 Plant pattern recognition receptors (PRRs)<br>1.3 Second Messengers in PAMP Signaling<br>1.4 Plant Hormone Signals in Plant Immune Signaling system<br>1.5 War between Host Plants and Pathogens and the Winner is …….?<br>2. PAMP signaling in Plant Innate Immunity<br>2.1 Classical PAMPs as Alarm Signals<br>2.2 Effector-like PAMPs<br>2.3 PAMPs found within Effectors<br>2.4 Toxins acting as PAMPs<br>2.5 PAMP-induced HAMPs (DAMPs/ MIMPs/ PAMP Amplifiers/ Endogenous Elicitors)<br>2.6 Bacterial PAMPs<br>2.7 Fungal PAMPs<br>2.8 Oomycete PAMPs<br>2.9 Viral Elicitors<br>2.10 Host-associated Molecular patterns (HAMPs) as Endogenous Elicitors<br>2. 11 Pattern Recognition Receptors (PRRs)<br>2.12 Transmembrane Proteins interacting with PRRs in PAMP-PRR Signaling Complex<br>2.13 PAMP triggers increased Transcription of PRR gene and Accumulation of PRR Protein<br>2.14 PAMPs induce Phosphorylation of PRRs  <br>2.15 Negative Regulation of PRR Signaling<br>2.16 Translocation of PRRs from Plasma Membrane to Endocytic Compartments<br>2.17 ERQC (for ENDOPLASMIC RETICULUM QUALITY CONTROL) Pathways in Biogenesis of PRRs<br>2.18 N-glycosylation of PRRs<br>2.19 Significance of PRRs in Innate Immunity<br>2.20 PAMPs-induced Early Signaling Events Downstream of PRRs<br>2.21 Different PAMPs and HAMPs may induce Similar Early Signaling Systems<br>2.22 Magnitude and Timing of Expression of early Signaling Systems may vary depending on specific PAMPs<br>2.23 PAMPs may differ in eliciting various Defense Responses<br>2.24 Synergism and Antagonism in Induction of Plant Immune Responses by PAMPs/HAMPs<br>2.25 Amount of PAMP/HAMP determines the Intensity of Expression of Defense Signaling Genes<br>2.26 Amount of PAMP available in the Infection Court may determine the Level of Induction of Immune Responses<br>2.27 PAMPs may trigger Different Signaling Systems <br />2.28 PAMPs may function Differently in Different Plants<br>2.29 Specificity of PAMPs in triggering Immune Responses in Plants<br>2.30 Role of PAMPs and Effectors in Activation of Plant Innate Immune Responses<br>2.31 Effectors may suppress PAMP-triggered Immunity<br>2.32 PAMP-induced Small RNA-mediated RNA Silencing<br>3. G-proteins as Molecular Switches in Signal Transduction <br>3.1 G-proteins switch on Plant Innate Immunity Signaling Systems<br>3.2 Heterotrimeric G-protein Signaling<br>3.3 Small G-proteins Signaling<br>3.4 Heterotrimeric G-protein Gα may act Upstream of Small G-protein in Immune Signaling <br>3.5 Different G-protein subunits in Heterotrimeric G-proteins play Distinct Roles in Plant Innate Immunity<br>3.6 Small G-proteins Activate Plant Innate Immunity<br>3.7 Small G-proteins may be involved in Susceptible Interactions<br>3.8 RAR1-SGT1-HSP90-HSP70 Molecular Chaperone Complex: a Core Modulator of Small G-protein-triggered Plant Innate Immunity<br>3.9 PAMP Signal may convert the G-proteins from their Inactive State to their Active State to trigger Immune Responses<br>3.10 PAMP-activated G-proteins switch on Calcium ion-mediated Immune Signaling System<br>3.11 G-proteins may trigger Efflux of Vacuolar Protons into Cytoplasm to activate pH-dependent Signaling Pathway<br>3.12 G-proteins switch on ROS Signaling System<br>3.13 G-proteins activate Nitric oxide Signaling System<br>3.14 Close relationship between G-proteins and MAPKs in Signal Transduction<br>3.15 G-proteins induce biosynthesis of polyamines which act as second messengers triggering early signaling events<br>3.16 G- proteins modulate Salicylic acid Signaling Pathway<br>3.17 G-proteins trigger Ethylene Signaling Pathway<br>3.18 G-proteins switch on Jasmonate Signaling System<br>3.19 G-proteins switch on Abscisic acid Signaling System<br>3.20 G-proteins may participate in Gibberellic acid Signaling<br />3.21 G-proteins participate in Brassinosteroid Signaling<br>3.22 Interplay between G-proteins and Auxin Signaling Systems<br>3.23 G-proteins Activate Defense-related Enzymes<br>4. Calcium Ion Signaling System: Calcium Signatures and Sensors<br>4.1 Calcium Signature in Plant Immune Signal Transduction System<br>4.2 Upstream Events leading to Activation of Ca2+ - permeable Channels <br>4.3 Ca2+ Influx Channels in Plant Cell Plasma Membrane<br>4.4 Ca2+ release Channels Involved in Releasing Stored Ca2+ in Vacuole and Endoplasmic Reticulum into cytosol<br>4.5 Ca2+ Efflux from Cytosol to Vacuole and Endoplasmic Reticulum (ER)<br>4.6 Plasma Membrane H+-ATPases in Ca2+ Signaling<br>4.7 Anion Channels in Ca2+ Influx and Increase in [Ca2+]cyt<br>4.8 K+ channels in Ca2+ Influx<br>4.9 K+/H+ exchange Response in Ca2+ Signaling System<br> 4.10 PAMPs and DAMPs may trigger Calcium Ion Influx/efflux through Different Ca2+ Channels   <br>4.11 Induction of Increases in Concentration, Oscillations and Waves in Cytoplasmic Calcium Ion ([Ca2+]cyt)<br>4.12 Ca2+ Sensors in Ca2+ Signal Transduction<br>4.13 Calmodulins  as Ca2+ Sensors<br>4.14 Calmodulin-binding  Proteins<br>4.15 Calmodulin-like proteins as Ca2+ Sensors<br>4.16 Calcineurin B- like Proteins as Ca2+ sensors<br>4.17 NADPH Oxidase as Calcium-binding Protein<br>4.18 Ca2+-binding Proteins without EF-Hands<br>4.19 Calcium-dependent Protein kinases as Ca2+ Sensors<br>4.20 Nuclear Free Calcium Ion ([Ca2+]nuc) in Ca2+ Signaling<br>4.21 Downstream Events in Ca2+ Signaling System <br>4.22 Importance of Calcium Signaling System in Activation of Plant Innate Immunity<br>5. Reactive Oxygen Species and Cognate Redox Signaling System in Plant Innate Immunity<br>5.1 Reactive Oxygen Intermediates Involved in Oxidative burst<br>5.2 Upstream Events in ROS Signaling System<br>5.3 ROS-Scavenging systems may be involved in Fine-tuning Accumulation of ROS<br>5.4 Site of Production of ROS<br>5.5 Biphasic ROS Production<br />5.6 ROS Plays a Central Role in Triggering Immune Responses<br>5.7 Interplay between ROS and Ca2+ Signaling System<br>5.8 Interplay between ROS and NO Signaling Systems<br>5.9 Interplay between ROS and MAPK Signaling Systems <br>5.10 Interplay between ROS and Salicylic acid Signaling Systems<br>5.11 Interplay between ROS and Ethylene Signaling Systems<br>5.12 Interplay between ROS and Jasmonate Signaling Systems<br>5.13 Interplay between ROS and Abscisic acid (ABA) Signaling Systems<br>5.14 ROS activates Phosphorylation/dephosphorylation Systems <br>5.15 Function of ROS in Ubiquitin-Proteasome System<br>5.16 ROS may Regulate Expression of Transcription Factors<br>5.17 Redox Signaling System<br>5.18 ROS Signaling System may activate Transcription of Defense Genes<br>5.19 Pathogens may cause Disease by Interfering with ROS Signaling System in Host Plants<br>6. Nitric oxide Signaling System in Plant Innate Immunity<br>6.1 Nitric Oxide as a Component of the Repertoire of Signals involved in Plant Immune Signaling System<br>6.2 PAMP-induced Biosynthesis of NO in Plants<br>6.3 Upstream Events in NO Production<br>6.4 Nitric Oxide-Target Proteins<br>6.5 Interplay between NO and Ca2+ Signaling Systems <br>6.6 Interplay between NO and ROS Signaling Systems<br>6.7 Role of NO in SA, JA, and Ethylene Signaling Systems<br>6.8 Role of NO in Protein S-Nitrosylation<br>6.9 Role of NO in Protein Nitration<br>6.10 Role of NO in Salicylic acid-regulated Systemic Acquired Resistance<br>7. Mitogen-activated Protein Kinase Cascades in Plant Innate Immunity<br>7.1 MAPK Signaling Three-Kinase Modules<br>7.2 MAP Kinases Involved in Plant Immune Responses<br>7.3 MAPK Kinases (MAPKKs) in Plant Immune Responses<br>7.4 MAPKK Kinase EDR1 Modulates SA-JA-ET Signaling <br>7.5 MAPK Pathways involved in Defense Signal Transduction may be interconnected<br />7.6 14-3-3 Protein Enhances Signaling Ability of MAPKKK in Activating Plant Innate Immune Response<br>7.7 Role of MAPKs in Priming Plants for Augmented Defense Gene Activation <br>7.8 PAMP Signals Activate MAP kinases<br>7.9 Signals and Signaling Systems Activating MAPK Cascades<br>7.10 MAPKs May Function Downstream of G-proteins, Ca2+, ROS, SA, ABA, and NO Signaling Pathways<br>7.11 Some MAPKs may act Upstream of SA, JA, and ET Signaling Pathways<br>7.12 Some MAP Kinases act Downstream of Phosphoinositide (PI) Signal Transduction Pathway<br>7.13 MAP Kinase Cascades may act either Upstream or Downstream of ROS Signaling System<br>7.14 MAP Kinases Positively or Negatively Regulate SA Signaling System<br>7.15 MAP Kinase Cascades activate JA Signaling System<br>7.16 Some MAP kinase Cascades are involved in Biosynthesis of Ethylene and Ethylene-mediated Signaling Systems<br>7.17 Involvement of MAP Kinase in Crosstalk between SA and JA/ET Signaling Systems<br>7.18 MAPK Phosphatases as Negative Regulators of MAP Kinases<br>7.19 MAP Kinase Cascades Modulate Phosphorylation of Transcription Factors to Trigger Transcription of Defense Genes<br>7.20 MAPKs Regulate Defense Gene Expression by Releasing Transcription Factors in the Nucleus<br>7.21 Role of MAPK Signaling Cascade in Triggering Phytoalexin Biosynthesis<br>8. Phospholipids Signaling System in Plant Innate Immunity<br>8.1 Biosynthesis of Phospholipids-derived Second Messengers<br>8.2 Phospholipids in Ca2+ Signaling System<br>8.3 Phosphatidic acid in G Proteins-mediated Signaling System<br>8.4 Phosphatidic acid in ROS Signaling System<br>8.5 Phospholipids in JA Signaling System<br>8.6 Phospholipid Signaling System in ABA Signaling Network<br>8.7 Phosphatidic acid in Phosphorylation/dephosphorylation System<br>9. Protein Phosphorylation and Dephosphorylation in Plant Immune Signaling Systems<br>9.1 Protein Phosphorylation plays Key Roles in Plant Immune Signal Transduction<br>9.2 Protein Phosphorylation is an Early PAMP/Elicitor-Triggered Event<br />9.3 Protein Phosphorylation is carried out by Different Protein Kinases<br>9.4 PAMPs/Elicitors activate Receptor-like Kinases<br>9.5 PAMP/Elicitor Induces Phosphorylation of Calcium-dependent Protein Kinases<br>9.6 PAMP/elicitor Triggers Phosphorylation of MAP Kinases<br>9.7 Role of 14-3-3 Proteins in Protein Phosphorylation<br>9.8 PAMP/Elicitor Triggers Phosphorylation of PEN Proteins<br>9.9 Protein Phosphorylation Involved in Early Defense Signaling Events Triggered by PAMPs/Elicitors<br>9.10 Phosphorylation of Proteins involved in H+ fluxes induced by PAMP/elicitor<br>9.11 Phosphorylation of Proteins involved in ROS Signaling System<br>9.12 Phosphorylation of Proteins Involved in Ethylene-Signaling System<br>9.13 Phosphorylation of Proteins involved in Salicylic acid Signaling System<br>9.14 Protein Phosphorylation in ABA Signaling System<br>9.15 Phosphorylation of Transcription Factors<br>9.16 Phosphorylation Events Induced by MAP Kinases in Various Signaling systems<br>9.17 Dephosphorylation induced by Phosphatases may negatively regulate Innate Immune Responses<br>10. Ubiquitin-Proteasome System-mediated Protein Degradation in Defense Signaling<br>10.1 Ubiquitin-Proteasome System in Plants<br>10.2 Ubiquitin-Proteasome in Jasmonate Signaling System<br>10.3 Ubiquitin-Proteasome in Ethylene Signaling System<br>10.4 Ubiquitin-Proteasome in SA Signaling System <br>10.5 Ubiquitin-Proteasome in R-Gene mediated Early Signaling System<br>10.6 Small Ubiquitin-like Modifier (SUMO) in Plant Immunity<br>10.7 Pathogens may subvert ubiquitin-proteasome system to cause Disease</p>

Rubrieken

    Personen

      Trefwoorden

        PAMP Signals in Plant Innate Immunity