International review of cell and molecular biology. V.266 /
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ISBN：9780123743756
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简介
Summary:
Publisher Summary 1
DESCRIPTION:
International Review of Cell & Molecular Biology presents current advances and comprehensive reviews in cell biology鈥攂oth plant and animal. Articles address structure and control of gene expression, nucleocytoplasmic interactions, control of cell development and differentiation, and cell transformation and growth. Authored by some of the foremost scientists in the field, each volume provides up-to-date information and directions for future research
Key Features
* Authored by some of the foremost scientists in the field
* Provides up-to-date information and directions for future research
* Valuable reference material for advanced undergraduates, graduate students and professional scientists
目录
Table Of Contents:
Contributors vii
CHAPTER ONE PHYSIOLOGICAL ROLES OF RIBOSOMAL PROTEIN S6: ONE OF ITS KIND 1
Oded Meyuhas
1. Introduction 2
2. General Background 3
2.1. Evolutionary conservation of rpS6 3
2.2. rpS6 is an indispensable ribosomal protein 4
3. Phosphorylation of rpS6 5
3.1. Stimuli inducing rpS6 phosphorylation 5
3.2. Signaling to rpS6 phosphorylation 13
4. Physiological Roles of rpS6 Phosphorylation 19
4.1. Global protein synthesis 19
4.2. Translational control of TOP mRNAs: The rise and fall of a myth 20
4.3. rpS6 phosphorylation as an effector of TORC1 in determining cell size 22
4.4. Cell proliferation 24
4.5. Glucose homeostasis 24
4.6. rpS6 phosphorylation as a diagnostic marker 25
5. Concluding Remarks and Future Perspectives 25
Acknowledgments 27
References 27
CHAPTER TWO MOLECULAR DOMAINS IN EPITHELIAL SALT CELLNaCl OF CRUSTACEAN SALT GLAND (ARTEMIA) 39
Frank R Conte
1. Introduction 40
2. Epithelium 40
2.1. Chloride cell or salt cell NaCl 41
2.2. Toxins to ionic regulation (cf. Conte, 1984) 41
2.3. Spatial arrangements of polar epithelium 44
3. Polar Domains 49
3.1. Cytoskeleton associated with polar domains 49
3.2. Genetic regulation of spatial distribution of polar domains 50
3.3. Death of larval salt gland 50
3.4. Model of larval salt gland: Polar domains of ion transporter (Na,K) and channel (Cl) in salt cellNaCl 52
4. Concluding Remarks 54
References 55
CHAPTER THREE NATRIURETIC PEPTIDES IN VASCULAR PHYSIOLOGY AND PATHOLOGY 59
Geoffrey E. Woodard and Juan A. Rosado
1. Introduction 60
2. Natriuretic Peptides and Their Receptors 61
2.1. Natriuretic peptides 61
2.2. Natriuretic peptide receptors 65
3. Functions of Natriuretic Peptides 67
3.1. Vascular effects of natriuretic peptides 67
3.2. Natriuretic peptides in cardiac physiology and pathology 69
3.3. Antiproliferative effects of natriuretic peptides 71
3.4. Natriuretic peptides and hypertension 72
3.5. Natriuretic peptides and oxidative stress 73
4. Further Aspects of Natriuretic Peptides in Cardiovascular Medicine 78
5. Concluding Remarks 80
References 81
CHAPTER FOUR NEW INSIGHTS INTO THE CELL BIOLOGY OF INSECT AXONEMES 95
C. Mencarelli, P. Lupetti, and R. Dallai
1. Introduction 96
2. Structural Organization of the Axoneme in Insect Cilia and Flagella 97
2.1. Flagellar axoneme: From 9+2 to various axoneme models 97
2.2. Ciliary axoneme 102
3. Molecular Composition of the Insect Axoneme 107
3.1. Structural features of axonemal tubulins 109
3.2. Dynein 121
3.3. Other axonemal components 125
4. Assembly of the Insect Axoneme 126
5. Axoneme Function 130
5.1. Flagellar motility 130
5.2. Role of the axoneme in sensory cilia 133
6. Perspectives 135
Acknowledgments 135
References 135
CHAPTER FIVE NEW INSIGHTS INTO THE MECHANISM OF PRECURSOR PROTEIN INSERTION INTO THE MITOCHONDRIAL MEMBRANES 147
Markus Hildenbeutel, Shukry J. Habib, Johannes M. Herrmann, and Doron Rapaport
1. Introduction 148
2. The Protein Import Machinery of Mitochondria 149
2.1. Translocation across and into the outer membrane 149
2.2. Translocation across and into the inner membrane 162
3. Mitochondrially Encoded Proteins 173
3.1. Insertion via the Oxa1 complex 174
3.2. Alternative insertion routes 176
4. Future Perspectives 177
References 177
CHAPTER SIX MOLECULAR BIOLOGY OF GIBBERELLINS SIGNALING IN HIGHER PLANTS 191
Hironori Itoh, Miyako Ueguchi-Tanaka, and Makoto Matsuoka
1. Introduction 192
2. DELLA Protein, a Repressor of GA Signaling 192
2.1. What is DELLA protein? 192
2.2. GA-dependent degradation of DELLA protein is a key event in GA signaling 195
2.3. 26S proteasome-dependent degradation of DELLA protein is targeted by SCFGID2/SLY1 E3 ubiquitin ligase 196
3. Identification of a GA Receptor, GID1 199
3.1. Characterization of gid 1 mutants in rice reveals the function of GID1 199
3.2. GID1 protein has GA-binding activity and forms complexes with DELLA protein in a GA-dependent manner 200
3.3. GID1 is a common GA receptor in two model plants: Rice and Arabidopsis 202
3.4. Is GID1 the only GA receptor in higher plants? 204
4. Additional Regulators of GA Signaling 205
4.1. O-GI-GlcNAc transferase is involved in GA signaling 205
4.2. Transcription factors directly regulate GA-responsive gene expression 208
5. A Model of GA Signaling 213
6. Concluding Remarks 215
References 215
CHAPTER SEVEN OOCYTE QUALITY AND MATERNAL CONTROL OF DEVELOPMENT 223
Namdori R. Mtango, Santhi Potireddy, and Keith E. Latham
1. Introduction 224
2. Oogenesis 225
2.1. Stages of oogenesis 225
2.2. Oocyte鈥攆ollicle cell interactions 227
2.3. Relevance to oocyte quality 229
3. Oocyte Activation 234
3.1. Molecular mechanisms 234
3.2. Comparative effects of natural and artificial activation on development 235
4. Oocyte Components Controlling Early Development 236
4.1. Spindle formation and function 237
4.2. Maternal mRNAs 239
4.3. Maternal proteins 250
4.4. Effects of maternal mitochondria 253
4.5. Effects of the maternal pronucleus 255
4.6. Effects of the ooplasm on paternal pronucleus function 256
5. Oocyte Polarity and Development 258
6. Maternal Nutrition and Diabetes Affecting Oocyte and Embryo Quality 259
7. Perspectives and Significance 261
Acknowledgments 262
References 262
Index 291
Contributors vii
CHAPTER ONE PHYSIOLOGICAL ROLES OF RIBOSOMAL PROTEIN S6: ONE OF ITS KIND 1
Oded Meyuhas
1. Introduction 2
2. General Background 3
2.1. Evolutionary conservation of rpS6 3
2.2. rpS6 is an indispensable ribosomal protein 4
3. Phosphorylation of rpS6 5
3.1. Stimuli inducing rpS6 phosphorylation 5
3.2. Signaling to rpS6 phosphorylation 13
4. Physiological Roles of rpS6 Phosphorylation 19
4.1. Global protein synthesis 19
4.2. Translational control of TOP mRNAs: The rise and fall of a myth 20
4.3. rpS6 phosphorylation as an effector of TORC1 in determining cell size 22
4.4. Cell proliferation 24
4.5. Glucose homeostasis 24
4.6. rpS6 phosphorylation as a diagnostic marker 25
5. Concluding Remarks and Future Perspectives 25
Acknowledgments 27
References 27
CHAPTER TWO MOLECULAR DOMAINS IN EPITHELIAL SALT CELLNaCl OF CRUSTACEAN SALT GLAND (ARTEMIA) 39
Frank R Conte
1. Introduction 40
2. Epithelium 40
2.1. Chloride cell or salt cell NaCl 41
2.2. Toxins to ionic regulation (cf. Conte, 1984) 41
2.3. Spatial arrangements of polar epithelium 44
3. Polar Domains 49
3.1. Cytoskeleton associated with polar domains 49
3.2. Genetic regulation of spatial distribution of polar domains 50
3.3. Death of larval salt gland 50
3.4. Model of larval salt gland: Polar domains of ion transporter (Na,K) and channel (Cl) in salt cellNaCl 52
4. Concluding Remarks 54
References 55
CHAPTER THREE NATRIURETIC PEPTIDES IN VASCULAR PHYSIOLOGY AND PATHOLOGY 59
Geoffrey E. Woodard and Juan A. Rosado
1. Introduction 60
2. Natriuretic Peptides and Their Receptors 61
2.1. Natriuretic peptides 61
2.2. Natriuretic peptide receptors 65
3. Functions of Natriuretic Peptides 67
3.1. Vascular effects of natriuretic peptides 67
3.2. Natriuretic peptides in cardiac physiology and pathology 69
3.3. Antiproliferative effects of natriuretic peptides 71
3.4. Natriuretic peptides and hypertension 72
3.5. Natriuretic peptides and oxidative stress 73
4. Further Aspects of Natriuretic Peptides in Cardiovascular Medicine 78
5. Concluding Remarks 80
References 81
CHAPTER FOUR NEW INSIGHTS INTO THE CELL BIOLOGY OF INSECT AXONEMES 95
C. Mencarelli, P. Lupetti, and R. Dallai
1. Introduction 96
2. Structural Organization of the Axoneme in Insect Cilia and Flagella 97
2.1. Flagellar axoneme: From 9+2 to various axoneme models 97
2.2. Ciliary axoneme 102
3. Molecular Composition of the Insect Axoneme 107
3.1. Structural features of axonemal tubulins 109
3.2. Dynein 121
3.3. Other axonemal components 125
4. Assembly of the Insect Axoneme 126
5. Axoneme Function 130
5.1. Flagellar motility 130
5.2. Role of the axoneme in sensory cilia 133
6. Perspectives 135
Acknowledgments 135
References 135
CHAPTER FIVE NEW INSIGHTS INTO THE MECHANISM OF PRECURSOR PROTEIN INSERTION INTO THE MITOCHONDRIAL MEMBRANES 147
Markus Hildenbeutel, Shukry J. Habib, Johannes M. Herrmann, and Doron Rapaport
1. Introduction 148
2. The Protein Import Machinery of Mitochondria 149
2.1. Translocation across and into the outer membrane 149
2.2. Translocation across and into the inner membrane 162
3. Mitochondrially Encoded Proteins 173
3.1. Insertion via the Oxa1 complex 174
3.2. Alternative insertion routes 176
4. Future Perspectives 177
References 177
CHAPTER SIX MOLECULAR BIOLOGY OF GIBBERELLINS SIGNALING IN HIGHER PLANTS 191
Hironori Itoh, Miyako Ueguchi-Tanaka, and Makoto Matsuoka
1. Introduction 192
2. DELLA Protein, a Repressor of GA Signaling 192
2.1. What is DELLA protein? 192
2.2. GA-dependent degradation of DELLA protein is a key event in GA signaling 195
2.3. 26S proteasome-dependent degradation of DELLA protein is targeted by SCFGID2/SLY1 E3 ubiquitin ligase 196
3. Identification of a GA Receptor, GID1 199
3.1. Characterization of gid 1 mutants in rice reveals the function of GID1 199
3.2. GID1 protein has GA-binding activity and forms complexes with DELLA protein in a GA-dependent manner 200
3.3. GID1 is a common GA receptor in two model plants: Rice and Arabidopsis 202
3.4. Is GID1 the only GA receptor in higher plants? 204
4. Additional Regulators of GA Signaling 205
4.1. O-GI-GlcNAc transferase is involved in GA signaling 205
4.2. Transcription factors directly regulate GA-responsive gene expression 208
5. A Model of GA Signaling 213
6. Concluding Remarks 215
References 215
CHAPTER SEVEN OOCYTE QUALITY AND MATERNAL CONTROL OF DEVELOPMENT 223
Namdori R. Mtango, Santhi Potireddy, and Keith E. Latham
1. Introduction 224
2. Oogenesis 225
2.1. Stages of oogenesis 225
2.2. Oocyte鈥攆ollicle cell interactions 227
2.3. Relevance to oocyte quality 229
3. Oocyte Activation 234
3.1. Molecular mechanisms 234
3.2. Comparative effects of natural and artificial activation on development 235
4. Oocyte Components Controlling Early Development 236
4.1. Spindle formation and function 237
4.2. Maternal mRNAs 239
4.3. Maternal proteins 250
4.4. Effects of maternal mitochondria 253
4.5. Effects of the maternal pronucleus 255
4.6. Effects of the ooplasm on paternal pronucleus function 256
5. Oocyte Polarity and Development 258
6. Maternal Nutrition and Diabetes Affecting Oocyte and Embryo Quality 259
7. Perspectives and Significance 261
Acknowledgments 262
References 262
Index 291
International review of cell and molecular biology. V.266 /
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