Machida / Lin / Tamanoi Signaling Pathways in Plants

1. Auflage 2014
ISBN: 978-0-12-802015-9
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, Band Volume 35, 298 Seiten

Reihe: The Enzymes

This special issue of The Enzymes is targeted towards researchers in biochemistry, molecular and cell biology, pharmacology, and cancer. This volume discusses signaling pathways in plants. - Contributions from leading authorities - Informs and updates on all the latest developments in the field

Autoren/Hrsg.

Machida, Yasunori

Lin, Chentao

Tamanoi, Fuyuhiko

Inhaltsverzeichnis

1;Front Cover;1
2;Signaling Pathways in Plants;4
3;Copyright;5
4;Contents;6
5;Contributors;10
6;Preface;12
7;Chapter One: Regulatory Networks Acted Upon by the GID1-DELLA System After Perceiving Gibberellin;16
7.1;1. Gibberellin Perception System in Higher Plants;17
7.2;2. Suppression of DNA-Binding Activity of TFs by DELLA (Trapping Function of DELLA);20
7.2.1;2.1. Phytochrome-Interacting Factor Family of Proteins Involved in Hypocotyl Elongation and Chlorophyll Biosynthesis;20
7.2.2;2.2. Alcatraz and Spatula Involved in Valve Margin Development and Cotyledon Expansion, Respectively;22
7.2.3;2.3. Squamosa Promoter Binding-Like Proteins Involved in Floral Transition;23
7.2.4;2.4. Ethylene-Insensitive 3 and EIN3-Like 1 Involved in the GA-Ethylene Crosstalk for Apical Hook Development;23
7.2.5;2.5. Brassinazole-Resistant 1 Involved in the GA-Brassinosteroid Crosstalk for Hypocotyl Elongation;24
7.2.6;2.6. Jasmonate ZIM Domain and MYC2 Proteins Involved in the GA-Jasmonate Acid Crosstalk Under Certain Conditions;25
7.3;3. Transcriptional Regulation of Downstream Genes Via the Interaction of DELLA with Their Promoters (Direct Targeting Fun...;26
7.3.1;3.1. Backgrounds;26
7.3.2;3.2. ABA-Insensitive 3 and ABI5 Involved in GA-Abscisic Acid Crosstalk;28
7.3.3;3.3. Indeterminate Domain Proteins Involved in the Feedback Regulation of GA Signaling;28
7.3.4;3.4. Botrytis-Susceptible Interactor and Its Related Proteins Involved in the Transrepression Activity of DELLA;30
7.4;4. Other Functions of DELLA Besides Transcriptional Regulation;31
7.4.1;4.1. Prefoldin 3 and PFD5 Involved in Cortical Microtubule Arrangement;31
7.4.2;4.2. D14 Involved in GA-Strigolactone Crosstalk;32
7.5;5. Future Perspectives;33
7.6;References;34
8;Chapter Two: Phosphorylation Networks in the Abscisic Acid Signaling Pathway;42
8.1;1. Introduction;43
8.2;2. SnRK2: A Core Component in ABA Signaling;45
8.2.1;2.1. Upstream Regulation of SnRK2 Activation;46
8.2.2;2.2. Diverse SnRK2 Substrates;47
8.2.3;2.3. CDPK Interacts with the SnRK2 Pathway;49
8.3;3. MAPK Cascades in ABA Signaling;50
8.3.1;3.1. MAPK Activation for Antioxidant Defense in ABA Signaling;53
8.3.2;3.2. MAPK Regulation in ABA-Mediated Seedling Development;54
8.3.3;3.3. Function of ABA-Inducible MAPKs;55
8.3.4;3.4. Regulation of MAPK Signaling in Guard Cells;56
8.4;4. Phosphoproteomic Approach to the Phosphorylation Network in ABA Signaling;57
8.4.1;4.1. Comparative Phosphoproteomics Using SnRK2 Mutants;59
8.4.2;4.2. Motif Analysis to Narrow Down SnRK2 Substrates;59
8.4.3;4.3. Prediction of the SnRK2-Dependent Protein Phosphorylation Network;60
8.5;5. Future Perspectives;61
8.6;Acknowledgments;62
8.7;References;62
9;Chapter Three: Action of Strigolactones in Plants;72
9.1;1. Introduction;73
9.2;2. Biosynthesis and Distribution of Strigolactones;73
9.2.1;2.1. Biosynthesis of SLs;73
9.2.2;2.2. Transport of SLs;75
9.3;3. The Strigolactone Signaling Pathway;75
9.3.1;3.1. The Leu-Rich Repeat F-Box Protein;75
9.3.2;3.2. The a/ß-Fold Hydrolase;78
9.3.3;3.3. The Clp Protease Family Protein;80
9.3.4;3.4. Other Proteins Involved in SL Signaling;82
9.3.5;3.5. Downstream Responses of SL Signaling in Shoot Branching;83
9.3.5.1;3.5.1. The SL-Mediated Transcription Response;83
9.3.5.2;3.5.2. SL-Regulated Auxin Polar Transport;84
9.3.6;3.6. Similarities and Differences of Signaling Pathways Between SLs and Other Plant Hormone;86
9.3.6.1;3.6.1. Ubiquitin Proteasome Systems of Plant Hormones;86
9.3.6.2;3.6.2. TPL/TPR Corepressors;90
9.4;4. Effect of Strigolactones on Plant Adaption to Environments;91
9.4.1;4.1. SLs Act as Communication Molecules in Plant Development;91
9.4.2;4.2. Cross talk Between SLs and Other Plant Hormones;93
9.5;References;94
10;Chapter Four: Peptide Ligands in Plants;100
10.1;1. Introduction;101
10.2;2. Clavata3/Embryo surrounding region;102
10.2.1;2.1. CLV3;102
10.2.2;2.2. TDIF;105
10.2.3;2.3. CLE40;105
10.2.4;2.4. CLE45;105
10.2.5;2.5. Other CLE Peptides;106
10.2.6;2.6. CLE Peptides in Other Species;106
10.3;3. Systemin;106
10.4;4. Hydroxyproline-Rich SlSys;107
10.5;5. Plant Elicitor Peptide;108
10.6;6. Phytosulfokine;108
10.7;7. Plant Peptide Containing Sulfated Tyrosine 1;109
10.8;8. Root Meristem Growth Factor;109
10.9;9. Inflorescence deficient in abscission;110
10.10;10. C-Terminally Encoded Peptide;111
10.11;11. Epidermal patterning factor/EPF Like;111
10.12;12. Lure;113
10.13;13. S-Locus Cysteine-Rich Protein/S-Locus Protein 11;114
10.14;14. Rapid Alkalinization Factor;115
10.15;15. Xylogen;116
10.16;16. Tapetum determinant1;116
10.17;17. Conclusions;117
10.18;References;118
11;Chapter Five: Florigen Signaling;128
11.1;1. Introduction;129
11.2;2. Identification of Florigen;131
11.3;3. Structure of the FT Protein;132
11.4;4. FT-Interacting Factors;134
11.5;5. Florigen Activation Complex;135
11.6;6. Molecular Mechanisms of FAC Formation: 14-3-3 as a Florigen Receptor;138
11.7;7. Gene Networks Downstream of Florigen;139
11.7.1;7.1. Direct Targets for FAC;139
11.7.2;7.2. Downstream Genes Identified in Transcriptome Analyses;140
11.8;8. Pleiotropic Functions of the FT Family;140
11.9;9. Molecular Function of the FT Protein;143
11.10;10. Intercellular Transport of FT;144
11.11;11. Photoperiodic Regulation of Florigen Gene Expression;145
11.11.1;11.1. Arabidopsis;146
11.11.2;11.2. Rice;149
11.12;12. Natural Variation in Flowering Time Genes;150
11.13;13. Conclusions;151
11.14;Acknowledgments;152
11.15;References;152
12;Chapter Six: Signaling Pathway that Controls Plant Cytokinesis;160
12.1;1. Introduction;161
12.2;2. The NACK-PQR Pathway: A MAP Kinase Cascade that Positively Regulates Plant Cytokinesis;165
12.2.1;2.1. A MAP Kinase Cascade Involved in Plant Cytokinesis;165
12.2.2;2.2. NPK1 MAPKKK and NACK1 Kinesin;165
12.2.3;2.3. Components in the MAPK Cascade Downstream of NPK1;168
12.3;3. Functions of Cytokinetic Kinesin NACK Are Dually Regulated by CDKs;169
12.3.1;3.1. Amplification of M-Phase-Specific NACK1 Transcription by CDKs;170
12.3.2;3.2. Repression of NACK1 Functions by CDKs During the Early M Phase;172
12.4;4. Effectors Controlled by the NACK-PQR Pathway;173
12.5;5. Future Prospects;174
12.6;Acknowledgments;175
12.7;References;175
13;Chapter Seven: Cryptochrome-Mediated Light Responses in Plants;182
13.1;1. Introduction;183
13.2;2. Physiological Responses Mediated by Plant Cryptochromes;185
13.2.1;2.1. Blue Light-Stimulated Photomorphogenesis;185
13.2.2;2.2. Photoperiodic Control of Flowering Time;187
13.2.3;2.3. Cryptochromes and Clock: Light Entrainment and Temperature Compensation;189
13.2.4;2.4. Light-Controlled Stomatal Opening and Development;191
13.2.5;2.5. The Functions of Cryptochrome in Other Plants;193
13.3;3. Perspectives;196
13.4;Acknowledgments;197
13.5;References;197
14;Chapter Eight: Multiple Roles of the Plasma Membrane H+-ATPase and Its Regulation;206
14.1;1. Introduction;207
14.2;2. H+-ATPase and Stomatal Movements;207
14.2.1;2.1. H+-ATPase Is a Key Enzyme in the Blue-Light-Induced Stomatal Opening Process;207
14.2.1.1;2.1.1. Blue-Light-Induced Stomatal Opening;207
14.2.1.2;2.1.2. Mechanism of Blue-Light-Induced Activation of the H+-ATPase;209
14.2.1.3;2.1.3. H+-ATPase Is the Limiting Factor of Light-Induced Stomatal Opening;210
14.2.2;2.2. H+-ATPase Is Involved in ABA-Induced Stomatal Closure;212
14.2.3;2.3. Other Factors Regulating the H+-ATPase in Guard Cells;213
14.2.3.1;2.3.1. Flowering Locus T;213
14.2.3.2;2.3.2. RPM1-Interacting Protein 4;213
14.3;3. H+-ATPase and Hypocotyl Elongation;214
14.4;4. Evolution of the H+-ATPase;216
14.5;5. Concluding Remarks;218
14.6;Acknowledgments;219
14.7;References;219
15;Chapter Nine: Structure and Function of the ZTL/FKF1/LKP2 Group Proteins in Arabidopsis;228
15.1;1. Introduction;228
15.2;2. The Circadian Clock Regulation by ZTL;229
15.3;3. Photoperiodic Flowering Regulation by FKF1;234
15.4;4. General LOV Chemistry;236
15.5;5. LOV Domain Photocycle;238
15.6;6. ZTL Group Protein Structure and Function;242
15.7;7. Perspectives;248
15.8;Acknowledgments;249
15.9;References;249
16;Author Index;256
17;Subject Index;292
18;Color Plate ;300

Leseproben

Chapter Two Phosphorylation Networks in the Abscisic Acid Signaling Pathway
Taishi Umezawa*; Fuminori Takahashi†; Kazuo Shinozaki†,1    * Faculty of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan
† RIKEN Center for Sustainable Resource Science, Tsukuba, Japan
1 Corresponding author: email address: [e-mail] Abstract
Abscisic acid (ABA) is one of the major phytohormones and regulates various processes in the plant life cycle, for example, seed development and abiotic/biotic stress responses. Recent studies have made significant progress in elucidating ABA signaling and established a simple ABA signaling model consisting of three core components: PYR/PYL/RCAR receptors, 2C-type protein phosphatases, and SnRK2 protein kinases. This model highlights the importance of protein phosphorylation mediated by SnRK2, but the downstream substrates of SnRK2 remain to be determined to complete the model. Previous studies have identified several SnRK2 substrates involving transcription factors and ion channels. Recently, SnRK2 substrates have been further surveyed by a phosphoproteomic approach, giving new insights on the SnRK2 downstream pathway. Other protein kinases, e.g., Ca2 +-dependent protein kinase (CDPK) and mitogen-activated protein kinase (MAPK), have been identified as ABA signaling factors. Some evidence suggests that the SnRK2 pathway partially interacts with CDPK or MAPK pathways. In this chapter, recent advances in ABA signaling study are summarized, primarily focusing on two major protein kinases, SnRK2 and MAPK. Challenges for further study of the ABA-dependent protein phosphorylation network are also discussed. Keywords Abscisic acid Protein phosphorylation Protein kinase Phosphoproteomics Signal transduction 1 Introduction
In the 1960s, abscisic acid (ABA) was discovered as one of the phytohormones [1]. Although ABA had been originally isolated as a growth-inhibiting substance, it was subsequently determined a phytohormone with widespread roles in various processes in the plant life cycle (Fig. 2.1). For example, ABA is essential for seed dormancy, maturation, germination, and postgermination growth [2]. Another important role of ABA is to induce stress responses in plants. ABA is necessary for drought tolerance in plants, because it regulates stomatal movement to prevent water loss and triggers gene expression, leading to cellular adaptation to low water potential [2–4]. Because such ABA responses are strictly regulated by cellular signal transduction systems, it is important to understand what is ABA signaling and how it is regulated in plant cells. Figure 2.1 Physiological functions of ABA in the plant life cycle. ABA are one of the major phytohormones and affect various physiological responses in developmental stages and stress adaptation. Initially, the study of ABA signaling was advanced by genetic screening of Arabidopsis mutants showing altered ABA response [2]. For example, a series of ABA-insensitive (ABI) mutants were isolated in the 1990s. Interestingly, the abi1-1 and abi2-1 mutants defected multiple ABA responses from seeds to adult plants, and ABI1 and ABI2 encode closely related 2C-type protein phosphatases (PP2Cs) [5–8]. Since these discoveries, the importance of protein phosphorylation in ABA signaling has been widely accepted. Recently, ABA signaling pathways are clearly identified and a core signaling model has emerged (Fig. 2.2). In a current model, three core components, PYR/PYL/RCAR, PP2C, and SNF1-related protein kinase 2 (SnRK2), compose the central module of ABA signaling [2,4,9–11]. The three components coordinate ABA signal output by regulating SnRK2 activity to induce cellular responses to ABA. It is believed that active SnRK2 can phosphorylate various substrates comprising a major protein phosphorylation network in ABA signaling. Figure 2.2 Core components of signal perception and transduction for ABA. Under normal conditions, the ABA signaling pathway is shut off because group A PP2Cs inactivate subclass III SnRK2s by direct dephosphorylation. When ABA is accumulated under stress conditions or in response to developmental cues, ABA is captured by PYR/PYL/RCAR proteins, and an ABA-bound form of PYR/PYL/RCAR interacts with group A PP2Cs to inhibit its phosphatase activity, resulting in an active form of SnRK2 that phosphorylates various downstream factors to transduce ABA signals and induce cellular responses. Although SnRK2 must be a major regulator in ABA signaling, some evidence suggests that other protein kinases, such as Ca2 +-dependent protein kinase (CDPK) and mitogen-activated protein kinase (MAPK), are also involved in ABA responses [12,13]. MAPK cascades are key signaling components in cellular responses to internal and external stimuli. A number of MAPK cascade components were isolated from various plants. In addition, a recent study has suggested that some MAPK cascades are regulated by the SnRK2 pathway in ABA signaling [14]. Each protein kinase is expected to be differentially activated to regulate its own protein phosphorylation cascade; therefore, it is important to understand how multiple protein kinases generate protein phosphorylation networks in ABA signaling. In general, to elucidate a signal transduction pathway involving protein kinases/phosphatases, it is necessary to characterize their upstream and downstream regulation. In the case of ABA signaling, a key protein kinase is SnRK2 and its upstream regulation has been mostly determined. The next question is to identify the downstream factors of SnRK2—its substrates—and the signal crosstalk of SnRK2 with other phosphorylation networks [11,15]. Although it is difficult to identify protein kinase substrates, progress has been made recently by a technical breakthrough in phosphoproteomics [14,16]. In this chapter, we review recent advances in ABA signaling studies, focusing primarily on the SnRK2 and MAPK protein phosphorylation networks. 2 SnRK2: A Core Component in ABA Signaling
The SnRK superfamily consists of three groups: SnRK1, SnRK2, and SnRK3 [17]. Each SnRK group has a well-conserved kinase domain similar to those of yeast sucrose nonfermenting 1 (SNF1) or mammalian AMPK (AMP-activated protein kinase). SnRK1 shows high similarity to SNF1 and AMPK and is believed to be a functional ortholog of SNF1 or AMPK [18]. However, SnRK2 and SnRK3 are likely to be different from SnRK1, considering both retain some specific C-terminal regions. In SnRK2, the C-terminal region contains a stretch of acidic residues, called the “acidic patch.” There is evidence that the C-terminal region plays an essential role in SnRK2 activation [19,20]. SnRK3 is quite different from other SnRKs, being regulated by Ca2 +-binding proteins, calcineurin B-like (CBL)/SCaBP. The C-terminal stretch of SnRK3 consists of regulatory domains functioning in autoinhibition [21,22]. These three SnRK families are well conserved in higher plants. For more details of the SnRK superfamily, refer to reviews [4,17,18,21,22]. Among SnRK superfamily proteins, SnRK2 plays a major part in ABA signaling. As stated above, the SnRK2 family is a plant-specific and well-conserved protein kinase family [4,17]. In the 1990s, an SnRK2 gene, PKABA1, was cloned from an ABA-treated wheat embryo cDNA library [23], and another SnRK2 gene, AAPK, was isolated from fava bean as an ABA-activated protein kinase in guard cells [24]. In both cases, further studies revealed that PKABA1 and AAPK are functional in ABA signaling, using a transient expression system in barley aleurone layers or guard cell protoplasts, respectively [25,26]. There are 10 members of SnRK2 in the Arabidopsis and rice genomes. Arabidopsis SnRK2s are designated as SRK2A–J and SnRK2.1–2.10 [17,27], and rice SnRK2s are designated as SAPK1–10 [20]. They are classified into three subclasses I, II, and III, and each subclass shows a different pattern of activation [20,28]. All SnRK2s are activated by osmotic stress, suggesting that SnRK2s play some role in osmotic stress signaling. Subclass III SnRK2s are strongly activated by ABA and are believed to be major ABA-activated protein kinases in plants. Subclass II SnRK2s are also activated by ABA, but their kinase activity is weaker than those of subclass III [20,28]. Physiological functions of SnRK2 in ABA signaling have been intensively investigated primarily in Arabidopsis. In Arabidopsis, subclass III contains three members, SRK2E, SRK2D, and SRK2I. These names may be confusing, considering SRK2E is also known as OPEN STOMATA 1 (OST1) or SnRK2.6 [17,27,29], and SRK2D and SRK2I are alternatively designated as SnRK2.2 and SnRK2.3, respectively [17]. In this review, they are abbreviated as SRK2E/OST1, SRK2D/SnRK2.2, and SRK2I/SnRK2.3, respectively. First, SRK2E/OST1 was identified as an ABA-activated protein kinase acting in guard cells...