Jeon International Review of Cell and Molecular Biology

1. Auflage 2014
ISBN: 978-0-12-800444-9
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, Band Volume 312, 288 Seiten

Reihe: International Review of Cell and Molecular Biology

International Review of Cell and Molecular Biology presents comprehensive reviews and current advances in cell and molecular biology. Articles address structure and control of gene expression, nucleocytoplasmic interactions, control of cell development and differentiation, and cell transformation and growth. The series has a world-wide readership, maintaining a high standard by publishing invited articles on important and timely topics authored by prominent cell and molecular biologists. - Authored by some of the foremost scientists in the field - Provides comprehensive reviews and current advances - Wide range of perspectives on specific subjects - Valuable reference material for advanced undergraduates, graduate students and professional scientists

Autoren/Hrsg.

Jeon, Kwang W.

Inhaltsverzeichnis

1;Front Cover;1
2;International Review Ofcell and Molecularbiology;4
3;Copyright;5
4;Contents;6
5;Contributors;10
6;Chapter One: Microtubule Organization and Microtubule-Associated Proteins in Plant Cells;12
6.1;1. Introduction;13
6.2;2. Overview of MT Arrays and Functions in Plant Cells;13
6.2.1;2.1. Cortical MTs;13
6.2.1.1;2.1.1. Functions of cortical MTs in cellular morphogenesis;15
6.2.1.2;2.1.2. Function of cortical MTs on organelle tethering and transport;19
6.2.2;2.2. Preprophase band;20
6.2.3;2.3. Mitotic spindle;21
6.2.4;2.4. Phragmoplast;23
6.3;3. MT-Associated Proteins in Arabidopsis;25
6.3.1;3.1. Definition and classification of MAPs;25
6.3.2;3.2. Conserved MAPs in eukaryotes;26
6.3.2.1;3.2.1. .-Tubulin complex;26
6.3.2.2;3.2.2. Augmin complex;28
6.3.2.3;3.2.3. Katanin;28
6.3.2.4;3.2.4. Kinesin;29
6.3.2.5;3.2.5. EB1;32
6.3.2.6;3.2.6. CLASP (TOG domain);32
6.3.2.7;3.2.7. MOR1 (MAP215 family, TOG domain);33
6.3.2.8;3.2.8. MAP65;34
6.3.2.9;3.2.9. TPX2;36
6.3.2.10;3.2.10. Formin family;36
6.3.3;3.3. Plant-specific MAPs;37
6.3.3.1;3.3.1. Cellulose synthase interacting;37
6.3.3.2;3.3.2. SPR2 (TOG domain);39
6.3.3.3;3.3.3. MAP70;40
6.3.3.4;3.3.4. AIR9;40
6.3.3.5;3.3.5. WVD2/WDL;40
6.3.3.6;3.3.6. RIP/MIDD family;41
6.3.3.7;3.3.7. RUNKEL (HEAT repeat);42
6.3.3.8;3.3.8. MPB2C;42
6.3.3.9;3.3.9. SPR1;42
6.3.3.10;3.3.10. MAP18/PCaP family;43
6.3.3.11;3.3.11. EDE1;44
6.3.3.12;3.3.12. MAP190;44
6.4;4. Conclusions and Future Directions;44
6.5;Acknowledgment;45
6.6;References;45
7;Chapter Two: ß-Catenin in Pluripotency: Adhering to Self-Renewal or Wnting to Differentiate?;64
7.1;1. Introduction;65
7.2;2. ß-Catenin in Canonical Wnt Signaling and Adhesion;66
7.2.1;2.1. ß-Catenin as transcriptional coactivator and mediator of adhesion;66
7.2.2;2.2. Regulation of ß-catenin adhesion and nuclear activities;68
7.3;3. ß-Catenin Activities in Regulation of Pluripotency;70
7.3.1;3.1. ß-Catenin and its partners for adhesion in pluripotency;70
7.3.2;3.2. ß-Catenin nuclear activities in regulation of pluripotency;73
7.3.2.1;3.2.1. ß-Catenin and Tcfs interactions in ESCs self-renewal;73
7.3.2.2;3.2.2. Key self-renewal regulators as nuclear partners of ß-catenin;76
7.3.2.3;3.2.3. ß-Catenin nuclear activities in differentiation induction;79
7.4;4. Conclusion;82
7.5;Acknowledgments;83
7.6;References;83
8;Chapter Three: Recent Advances in Molecular and Cell Biology of Testicular Germ-Cell Tumors;90
8.1;1. Introduction;91
8.2;2. Epidemiology and Risk Factors;91
8.3;3. Histopathology;92
8.4;4. Prognostic and Diagnostic Markers;95
8.4.1;4.1. Serum tumor markers in TGCTs;95
8.4.2;4.2. Newly discovered biomarkers detected by immunohistochemistry in TGCT subtypes;96
8.5;5. Therapy;101
8.5.1;5.1. Aurora-kinase inhibitors;101
8.5.2;5.2. Tyrosine-kinase inhibitors;102
8.5.3;5.3. Angiogenesis inhibitors;105
8.6;6. MicroRNAs in TGCTs;106
8.7;7. Conclusions and Perspectives;107
8.8;References;107
9;Chapter Four: New Insight into the Origin of IgG-Bearing Cells in the Bursa of Fabricius;112
9.1;1. Introduction;113
9.2;2. Structural Organization and Functions of the Bursa of Fabricius;114
9.2.1;2.1. Anatomy and histology of the bursa of Fabricius;114
9.2.2;2.2. Ontogeny of the bursa of Fabricius;114
9.2.3;2.3. Functions of the bursa of Fabricius;117
9.2.3.1;2.3.1. Major site for B-cell development;117
9.2.3.2;2.3.2. Major site for B-cell diversification;117
9.2.3.3;2.3.3. Major trapping site for environmental antigens;118
9.3;3. IgG-Bearing Cells in the Bursa of Fabricius;120
9.3.1;3.1. IgG-containing cells in the bursa of Fabricius;120
9.3.1.1;3.1.1. Ontogeny of IgG-containing cells;121
9.3.1.2;3.1.2. Ag-dependent development of IgG-containing cells;125
9.3.1.3;3.1.3. Absence of IgG biosynthesis by IgG-containing cells;125
9.3.1.4;3.1.4. Role of MIgG in the development of IgG-containing cells in the medulla of bursal follicles;127
9.3.1.5;3.1.5. Morphological characteristics of IgG-containing cells in the medulla of bursal follicles;130
9.3.1.6;3.1.6. Functions of IgG-containing cells in the medulla of bursal follicles;132
9.3.2;3.2. IgG+ B cells in the bursa of Fabricius;133
9.3.2.1;3.2.1. Ontogeny of IgM+IgG+ B cells;133
9.3.2.2;3.2.2. Ag-dependent development of IgM+IgG+ B cells;134
9.3.2.3;3.2.3. Absence of IgG biosynthesis by IgM+IgG+ B cells;136
9.3.2.4;3.2.4. Role of MIgG in the development of IgM+IgG+ B cells;137
9.3.2.5;3.2.5. Changes of bursal microenvironment after hatching;137
9.3.2.6;3.2.6. Functions of IgM+IgG+ B cells;139
9.4;4. Concluding Remarks;140
9.5;Acknowledgments;143
9.6;References;144
10;Chapter Five: Biological Mechanisms Determining the Success of RNA Interference in Insects;150
10.1;1. Introduction;151
10.2;2. RNAi Pathway and Small dsRNAs;152
10.3;3. Biological Functions of smRNAs in Insects;153
10.3.1;3.1. Antiviral role of siRNAs;153
10.3.2;3.2. miRNA pathway regulates different physiological processes in insects;154
10.3.3;3.3. piRNAs in controlling mobile genetic elements in insects;155
10.4;4. Dcr and Ago Proteins;155
10.5;5. Systemic RNAi;158
10.5.1;5.1. dsRNA-uptake mechanisms;159
10.5.2;5.2. Amplification of the RNAi signal;160
10.6;6. Species and Tissue Dependency of RNAi in Insects;161
10.7;7. RNAi as a Tool to Study and Control Insect Populations;162
10.7.1;7.1. RNAi in insect pest management;163
10.7.2;7.2. RNAi-based control of viral spread;164
10.8;8. Regulation of sysRNAi in Insects: Lessons Learned from Locusts;165
10.8.1;8.1. Sensitive sysRNAi responses of locusts;165
10.8.2;8.2. Tissue dependence of sysRNAi in locusts;167
10.8.3;8.3. Insensitivity of locusts to orally delivered dsRNA;167
10.9;9. Conclusions and Future Perspectives;168
10.10;References;170
11;Chapter Six: Canonical and Noncanonical Roles of Par-1/MARK Kinases in Cell Migration;180
11.1;1. Introduction;181
11.2;2. Canonical Roles of Par-1/MARK in Cell Migration I: MTs;182
11.2.1;2.1. Par-1/MARK proteins;182
11.2.2;2.2. Regulation of MTs by Par-1/MARK;184
11.2.3;2.3. MT dynamics in directed cell migration;185
11.2.4;2.4. Par-1/MARK, MTs, and cell migration;187
11.2.4.1;2.4.1. Nonneuronal cell migration;187
11.2.4.2;2.4.2. Neuronal cell migration;188
11.3;3. Canonical Roles of Par-1/MARK in Cell Migration II: Cell Polarity;190
11.3.1;3.1. Cell polarity proteins in cell migration;190
11.3.2;3.2. Cell polarity and Par-1/MARK regulation of Drosophila border cell migration;191
11.3.2.1;3.2.1. Cell polarity and the border cell model of collective migration;191
11.3.2.2;3.2.2. Role of Par-1 in border cell migration and polarity;194
11.3.3;3.3. Par-1/MARK and regulation of directional protrusions in migrating cells;195
11.4;4. Noncanonical Roles of Par-1/MARK in Cell Migration;197
11.4.1;4.1. Wnt pathways, Par-1/MARK, and cell movement during development;197
11.4.2;4.2. Par-1/MARK regulation of myosin during collective border cell migration;199
11.4.3;4.3. Role of Par-1/MARK in H. pylori CagA-dependent cell migration;201
11.5;5. Concluding Remarks;202
11.6;Acknowledgments;203
11.7;References;203
12;Chapter Seven: Insights into the Mechanism for Dictating Polarity in Migrating T-Cells;212
12.1;1. Introduction;213
12.2;2. G-Protein-Coupled Receptors;217
12.3;3. Adhesion Receptors and Associated Proteins;219
12.3.1;3.1. Integrins (LFA-1);219
12.3.2;3.2. Rap1/RAPL/Mst1;221
12.3.3;3.3. Talin-1, kindlin-3;222
12.3.4;3.4. a-Actinin;223
12.3.5;3.5. SHARPIN;223
12.4;4. Membrane Recycling/Organelles;224
12.5;5. Signaling Molecules;226
12.5.1;5.1. Rho-family GTPases;226
12.5.1.1;5.1.1. Rho/Rho-kinase;227
12.5.1.2;5.1.2. Rac;230
12.5.1.3;5.1.3. Cdc42;232
12.5.2;5.2. PIP-2/PIP5K;233
12.5.3;5.3. Phospholipase C;236
12.5.4;5.4. Calcium;237
12.5.5;5.5. PIP-3, PI 3-kinase;238
12.5.6;5.6. Janus kinases;240
12.5.7;5.7. PKC isoforms;241
12.5.8;5.8. ERK/MAPK;242
12.6;6. Cytoskeleton;243
12.6.1;6.1. Microtubules;244
12.6.2;6.2. Actin;246
12.6.2.1;6.2.1. Formins;247
12.6.2.2;6.2.2. WASP, N-WASP, WAVE, WIP, Arp2/3;248
12.6.2.3;6.2.3. Coronin-1;249
12.6.2.4;6.2.4. Ezrin/radixin/moesin;250
12.6.2.5;6.2.5. Myosin II;253
12.6.2.6;6.2.6. L-plastin;255
12.6.2.7;6.2.7. Cofilin;256
12.6.3;6.3. Septins;257
12.7;7. Polarity Proteins;258
12.7.1;7.1. Scribble/Dlg;259
12.7.2;7.2. Rap1 and the Par complexes;259
12.8;8. Membrane Microdomains (Rafts);260
12.8.1;8.1. Gangliosides;262
12.8.2;8.2. Flotillins;263
12.9;9. Self-Organizing Aspects of T-Cell Polarity;265
12.10;10. Concluding Remarks;267
12.11;Acknowledgments;269
12.12;References;269
13;Index;282
14;Color Plate;289

Leseproben

Chapter One Microtubule Organization and Microtubule-Associated Proteins in Plant Cells
Takahiro Hamada1    Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Tokyo, Japan
1 Corresponding author: email address: [e-mail] Abstract
Plants have unique microtubule (MT) arrays, cortical MTs, preprophase band, mitotic spindle, and phragmoplast, in the processes of evolution. These MT arrays control the directions of cell division and expansion especially in plants and are essential for plant morphogenesis and developments. Organizations and functions of these MT arrays are accomplished by diverse MT-associated proteins (MAPs). This review introduces 10 of conserved MAPs in eukaryote such as ?-TuC, augmin, katanin, kinesin, EB1, CLASP, MOR1/MAP215, MAP65, TPX2, formin, and several plant-specific MAPs such as CSI1, SPR2, MAP70, WVD2/WDL, RIP/MIDD, SPR1, MAP18/PCaP, EDE1, and MAP190. Most of the studies cited in this review have been analyzed in the particular model plant, Arabidopsis thaliana. The significant knowledge of A. thaliana is the important established base to understand MT organizations and functions in plants. Keywords Plants MAPs Microtubule Cortical microtubules Preprophase band Mitotic spindle Phragmoplast Arabidopsis thaliana 1 Introduction
Animals and plants have lots of differences. At the cellular level, cell motility is one of the prominent differences. For example, animal cells move independently and occupy specific positions during embryogenesis. In contrast, plant cells remain in place during embryogenesis, being confined by their cell wall. To accomplish morphogenesis and developments, plants control the directions of cell division in principle. Because the relative positions of cells never change after cell division, differentiation relies on cell-autonomous programs and strong-signaling cues between cells. In parallel, plant cells start expansion to proper sizes and shapes. Plant microtubules (MTs) and MT-associated proteins (MAPs) regulate both cell division and expansion. To enact morphogenesis, plants have evolved plant-specific MT arrays. Here, I review the properties and functions of MAPs that have been characterized in plants. I organize the review in two sections: MT arrays (Section 2) and MAPs (Section 3). 2 Overview of MT Arrays and Functions in Plant Cells
Plant cells have four prominent MT arrays: cortical MTs, preprophase band (PPB), mitotic spindle, and phragmoplast (Fig. 1.1). Briefly, cortical MTs regulate the direction of cell expansion and the other three MT arrays mediate cell division including the specification of its orientation. Organization and function of these MT arrays are described here. Figure 1.1 Microtubule arrays in plant cells. Cortical microtubules appear in interphase cells. Preprophase band (PPB) appears during the late G2 phase and prophase. Spindle microtubules nucleate around a nucleus and form bipolar mitotic spindle during metaphase to anaphase. Phragmoplast appears in telophase. Photos of each microtubule array in tobacco BY-2 cells were shown in right. 2.1 Cortical MTs
Plant cells usually have a large vacuole at the center and thin layer of cytoplasm at the periphery. In peripheral cytoplasm, many dynamic MTs localize immediately adjacent to the plasma membrane forming an almost two-dimensional cortical array called “cortical MTs” (i.e., in the cell cortex). Using live cell imaging methods, cortical MTs are readily observed and their behavior has been well characterized. The dynamics described below has been examined mainly at the hypocotyl epidermal cells of Arabidopsis thaliana but with support from other cell types, species, and other mitotic MT arrays and is taken as generally true for plants. In cells, MT nucleation (i.e., the initiation of polymerization) occurs at the site of ?-tubulin complex. In animal cells, many of these complexes are packed into foci called “MT-organizing centers” (e.g., the centrosome), but in plant cells, the complexes are dispersed throughout the cell. Often, a complex binds to the side of an extant MT, but sometimes a complex binds to an as-yet-undefined site in the cortex. From the side of an extant MT, a nucleated MT elongates either at an angle around 30° (Murata et al., 2005), thereby forming a branch, or parallel to the extant one, thereby forming a bundle (Chan et al., 2009). Similar to the cytoplasmic MTs of animal cells, cortical MTs in plants exhibit dynamic instability, with repeating phases of polymerization (i.e., growth) and disassembly (i.e., shrinkage) separated by pauses, catastrophes, and rescues. A catastrophe defines the sudden change from growth to shrinkage and a rescue defines the reverse. In addition to these dynamics, MT severing is occasionally observed. Growing MTs often encounter another MT at the virtual two-dimensional cortical array. The consequences of the encounter include bundling, catastrophe, or crossing. The choice among these behaviors depends on a considerable extent on the angle between them. Bundling is favored for angles of 30° and less, whereas catastrophe and crossing predominate for larger angles (Dixit and Cyr, 2004). The bundling mechanism is well adapted to “search and capture model,” which MTs repeat growth and shrinkage phases until reaching a given target. Although the MT itself has intrinsic dynamic instability and nucleation ability, MTs in cells are regulated by hundreds of MAPs, enriching the scope of MT behavior. In principle, some molecules should be bound tightly to the plasma membrane. This binding might be mediated by several candidates, including CSI1, CLASP, and PLD (Ambrose and Wasteneys, 2008; Gardiner et al., 2001; Gu et al., 2010). To regulate MT dynamic instability, relevant candidates include TOG domain-containing proteins such as MOR1, SPR2 (SPIRAL2), and CLASP. Both MOR1 and SPR2 stimulate MT dynamics directly, as confirmed in vivo and in vitro (Hamada et al., 2009; Kawamura and Wasteneys, 2008; Yao et al., 2008). CLASP has multiple functions for the cortical array, both increasing cortical MT attachment to the membrane and stabilizing cortical MTs’ cell edges (Ambrose and Wasteneys, 2008; Ambrose et al., 2011). MAP65 and WVD2 (Wave-Dampened 2)/WDL (WVD2-like) families are characterized as MT-bundling factors (Jiang and Sonobe, 1993; Perrin et al., 2007). The mutants of MOR1, SPR2, CLASP, ?-tubulin complex, and katanin complex have twisting macroscopic phenotypes that caused by the change of MT array orientation from transverse to oblique in young elongating cells. Similar phenotypes are often observed in mutants of other MAPs, such as EB1, MAP70, and WVD2/WDL (Bisgrove et al., 2008; Korolev et al., 2007; Yuen et al., 2003), indicating that these MAPs are involved in cortical MT organization to keep specific cell-wide orientation, such as transverse to the long axis of the organ. 2.1.1 Functions of cortical MTs in cellular morphogenesis Plant cells have two types of growth: “diffuse growth,” which occurs in most cell types, and “tip growth,” which occurs in specialized cell types such as pollen tubes and root hairs. Although semirigid cell walls surround plant cells, outward high turgor pressure enlarges by deforming relatively extensible regions of their cell wall. In the case of tip growth, expansion is confined to the cell tip, which has a sufficiently extensible cell wall to deform under turgor pressure. In contrast, with diffuse growth, expansion takes place over the entire surface of the cell, or majority thereof. Diffuse growth is typically anisotropic. Expansion rate between maximal and minimal directions often exceeds an order of magnitude or even more. For this type of growth, cortical MTs play a prominent role in determining the direction of expansion. The anisotropic nature of diffuse growth depends to a large extent on the orientation of cellulose microfibrils. When microfibrils align in one direction within the cell wall, encircling a cell like a hoop, the cell expands perpendicular to the net orientation of the microfibrils (Fig. 1.2A). When the direction of cellulose microfibrils is random, the cell expands isotropically, eventually becoming spherical (Fig. 1.2B). To shape long extended cells like typical root and hypocotyl plant cells, cellulose microfibrils are located transversely against the longitudinal direction of expansion. Figure 1.2 Anisotropic nature of diffuse growth in plant cells. Cortical microtubules control the direction of cellulose microfibrils. (A) Anisotropic growth occurs when cellulose microfibrils align in one direction. (B) Cell becomes spherical when the direction of cellulose microfibrils is random. The relationship between cellulose microfibrils and MTs was first recognized in the early 1960s, both from the spherical cells that result when elongating Nitella axillaris internode cells is exposed to the MT inhibitor colchicine (known then as a spindle fiber-disorganizing agent) (Green, 1962), and from the parallel alignments of cellulose...