Cell junctions : adhesion, development, and disease

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Title:

Publication Information:

Weinheim, GW : Wiley-VCH, 2008

Physical Description:

xv, 301 p. : ill. (some col.) ; 25 cm.

ISBN:

9783527318827

Subject Term:

Cell junctions

Added Author:

LaFlamme, Susan E.

Kowalczyk, Andrew P.

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Library	Item Barcode	Call Number	Material Type	Item Category 1	Status
Searching... PSZ JB	30000010222731	QH603.C4 C44 2008	Open Access Book	Book	Searching... Unknown

This long-awaited, first comprehensive book on this topic of fundamental importance in our understanding of cancer begins with an overview of cellular junctions, before covering cell-matrix junctions, cell-cell junctions and cell-matrix and cell-cell adhesion in separate sections.
Of high interest to cell and molecular biologists, cancer researchers, oncologists, biochemists, pharmaceutists and those working in the pharmaceutical industry.

Author Notes

Susan LaFlamme is a professor in the Center for Cell Biology and Cancer Research at the Albany Medical College in Albany NY. She obtained her B.A. from Barnard College and her PhD from Columbia University in New York NY, USA. Professor LaFlamme has received many grants for her studies on integrin signaling and has published extensively in this area. She has served on review panels for the National Institutes of Health, the American Cancer Society and the American Heart Association.

Andrew Kowalczyk is an Associate Professor for Cell Biology and Dermatology at Emory School of Medicine in Atlanta GA, USA. Dr. Kowalczyk obtained his PhD at Albany Medical School in Albany NY and carried out postdoctoral studies at Northwestern University Medical School in Chicago IL, USA. He has received numerous grants and awards and has published extensively in the area of cell adhesion. He has served on review panels for the National Institutes of Health and the American Heart Association, and on several advisory committees for the Society for Investigative Dermatology.

Asoka Banno and Mark H. GinsbergYoungdong Yoo and Jun-Lin GuanDavid A. Tumbarello and Christopher E. TurnerChrista L. Cortesio and Keefe T. Chan and Anna HuttenlocherSusan E. LaFlamme and Feng Shi and Jane SottileKristina Kligys and Kevin Hamill and Jonathan C. R. JonesPatricia J. KeelyLaura J. Lewis-Tuffin and Panos Z. AnastasiadisDeana M. Ferreri and Peter A. VincentMichael KovalCara J. Gottardi and Carien M. NiessenAnsgar Schmidt and Peter J. KochChristine M. Chiasson and Andrew P. KowalczykC. Michael DiPersio

Preface	p. V
List of Contributors	p. XIII
Part 1 Cell-Matrix Junctions
1 The Ins and Outs of Integrin Signaling	p. 3
1.1 General Overview	p. 3
1.1.1 Integrin Receptors	p. 3
1.1.2 Functions	p. 4
1.2 Integrin Activation	p. 5
1.2.1 Definition	p. 5
1.2.1.1 Platelets	p. 6
1.2.1.2 Leukocytes	p. 6
1.2.2 Structural Basis of Activation	p. 6
1.2.2.1 Extracellular Rearrangements	p. 7
1.2.2.2 Transmembrane Propagation	p. 7
1.2.2.3 Intracellular Rearrangements	p. 8
1.2.2.4 Interactions at the Integrin Cytoplasmic Domains	p. 9
1.2.3 Regulation of Integrin Activation	p. 13
1.2.4 Future Research Directions	p. 16
References	p. 18
2 Integrin Signaling Through Focal Adhesion Kinase	p. 25
2.1 Introduction	p. 25
2.2 Structure of FAK	p. 26
2.3 Regulation of FAK Activity	p. 28
2.3.1 Activation of FAK	p. 28
2.3.2 Inhibition of FAK Activity	p. 30
2.4 Regulation of Cellular Functions by FAK Signaling Pathways	p. 30
2.4.1 Cell Adhesion and Spreading	p. 31
2.4.2 Cell Migration and Invasion	p. 32
2.4.3 Cell Survival and Proliferation	p. 36
2.5 Recent Analysis of FAK Functions In Vivo	p. 37
2.6 Conclusions	p. 39
Acknowledgment	p. 39
References	p. 39
3 The Paxillin Family and Tissue Remodeling	p. 47
3.1 Focal Adhesions and the Paxillin Superfamily	p. 47
3.1.1 Focal Adhesions	p. 47
3.1.2 The Paxillin Superfamily	p. 49
3.1.3 Structure of Paxillin	p. 50
3.1.4 Structure of Hic-5	p. 51
3.2 The Paxillin Superfamily and Tissue Remodeling	p. 52
3.2.1 Epithelial-Mesenchymal Transformation	p. 52
3.2.2 Integrin-Mediated Signaling and EMT	p. 53
3.2.3 Paxillins [alpha] and [delta] in EMT	p. 56
3.2.4 Hic-5 and EMT	p. 58
References	p. 60
4 Adhesion Dynamics in Motile Cells	p. 71
4.1 Introduction	p. 71
4.2 Focal Adhesion Dynamics	p. 72
4.2.1 Focal Adhesion Composition	p. 73
4.2.2 Mechanisms of Focal Adhesion Assembly	p. 74
4.2.2.1 Rho GTPases	p. 75
4.2.2.2 Talin and Phosphoinositides	p. 75
4.2.3 Mechanisms of Focal Adhesion Disassembly	p. 75
4.2.3.1 Calpain	p. 76
4.2.3.2 Tyrosine Phosphorylation and Contractile Machinery	p. 76
4.3 Podosome and Invadopodia Dynamics	p. 76
4.3.1 Podosome and Invadopodia Architecture	p. 77
4.3.2 Molecular Mechanisms of PTA Assembly	p. 78
4.3.2.1 Actin Regulatory Proteins	p. 78
4.3.2.2 Rho GTPases	p. 79
4.3.2.3 Signaling Molecules	p. 79
4.3.3 Molecular Mechanisms of PTA Disassembly	p. 80
4.4 Summary	p. 80
Acknowledgments	p. 81
References	p. 81
5 Integrin Trafficking	p. 89
5.1 Introduction	p. 89
5.2 Historical Perspective	p. 89
5.3 Clathrin versus Lipid Rafts	p. 90
5.4 Internalization of Occupied versus Unoccupied Integrins	p. 91
5.5 Regulation of Integrin Trafficking	p. 92
5.6 The Role of Integrin Cytoplasmic Domains	p. 94
5.7 Integrin-Dependent Endocytosis of Microbial Pathogens	p. 95
5.8 Regulation of Cell Adhesion and Migration by Integrin Trafficking	p. 96
5.9 The Regulation of Integrin Trafficking by Cell Adhesion	p. 96
5.10 Integrin Trafficking and ECM Remodeling	p. 98
5.11 Conclusions	p. 100
Acknowledgments	p. 101
References	p. 101
6 Hemidesmosomes and their Components: Adhesion versus Signaling in Health and Disease	p. 109
6.1 Introduction	p. 109
6.2 The Structural Components of the Hemidesmosome	p. 110
6.2.1 The Plaque Proteins	p. 110
6.2.1.1 Plectin	p. 110
6.2.1.2 BP230	p. 112
6.2.2 Membrane Elements	p. 112
6.2.2.1 [alpha]6[beta]4 Integrin	p. 112
6.2.2.2 BP180	p. 114
6.2.2.3 CD151	p. 115
6.3 Laminin-332	p. 115
6.4 Hemidesmosome Assembly and Disassembly	p. 116
6.5 Hemidesmosomes and Disease	p. 118
6.5.1 Inherited Skin Diseases Involving Hemidesmosome Proteins	p. 118
6.5.1.1 Disease Involving [alpha]6[beta]4 Integrin	p. 118
6.5.1.2 Disease Involving Plectin	p. 119
6.5.1.3 Disease Involving BP180	p. 119
6.5.1.4 Disease Involving CD151	p. 120
6.5.1.5 Disease Involving Laminin-332	p. 120
6.5.2 Autoimmune Diseases Associated with Hemidesmosomes	p. 121
6.5.2.1 BP and Related Diseases	p. 121
6.5.2.2 Cicatricial Pemphigoid	p. 122
6.5.2.3 Autoimmune Diseases Involving [alpha]6[beta]4 Integrin	p. 122
6.6 [alpha]6[beta]4 Integrin and Laminin-332 Expression in Cancer	p. 123
6.7 Signaling by the [alpha]6[beta]4 Integrin in Pathological States and Wound Healing	p. 123
6.8 Laminin-332, [alpha]6[beta]4 Integrin and Migration	p. 125
6.9 Conclusions	p. 126
References	p. 126
7 Cell Matrix Adhesion in Three Dimensions	p. 135
7.1 Introduction	p. 135
7.2 Model 3D Matrices for Investigations of Cell Behavior	p. 136
7.2.1 Matrigel/Reconstituted Basement Membrane (rBM)	p. 136
7.2.2 Collagen Gels	p. 136
7.2.3 Fibrin Gels	p. 138
7.2.4 Cell-Derived Fibronectin-Based Matrices	p. 138
7.2.5 Engineered 3D Matrices and Microfluidic Chambers	p. 138
7.3 Cell Behavior and Adhesive Structures Differ between 3D and 2D Matrices	p. 139
7.4 "Compliancy" or Elastic Modulus Determines Cellular Response to ECMs	p. 140
7.4.1 Cellular Contractility and the Response to Matrix Compliance	p. 141
7.4.2 Rho Regulates the Cytoskeleton and Contractility	p. 141
7.4.3 Rho/ROCK, Contractility, and Focal Adhesion Formation	p. 142
7.4.4 Focal Adhesions as Transducers of Biophysical Signals	p. 143
7.5 A Model for Cellular Response to 3D Matrices Varying in Compliance	p. 144
Acknowledgments	p. 146
References	p. 146
Part 2 Cell-Cell Junctions
8 Armadillo Repeat Proteins at Epithelial Adherens Junctions	p. 153
8.1 Introduction	p. 153
8.2 [beta]-Catenin	p. 156
8.3 Plakoglobin	p. 158
8.4 p120-Catenin	p. 159
8.5 The Role of Armadillo Repeat Proteins and AJs in Cancer	p. 163
8.6 Conclusions	p. 165
References	p. 165
9 Signaling To and Through The Endothelial Adherens Junction	p. 169
9.1 Introduction	p. 169
9.2 Cadherins	p. 170
9.2.1 VE-Cadherin Extracellular Domain	p. 173
9.2.2 Interaction of Cadherin Cytoplasmic Domain and Catenins	p. 174
9.2.2.1 VE-Cadherin Juxtamembrane Region and p120	p. 174
9.2.2.2 VE-Cadherin Catenin Binding Domain	p. 176
9.3 Phosphorylation and Junction Assembly/Disassembly	p. 179
9.3.1 Tyrosine Phosphorylation of Endothelial AJ Proteins	p. 180
9.3.2 Serine/Threonine Phosphorylation of Endothelial AJ Proteins	p. 182
9.4 Small GTPases and Junction Assembly	p. 183
9.4.1 Rho GTPases	p. 183
9.4.2 Rap1 GTPase	p. 186
9.5 Conclusions	p. 187
References	p. 187
10 Gap Junctions: Connexin Functions and Roles in Human Disease	p. 197
10.1 Introduction	p. 197
10.2 Connexin Structure and Assembly	p. 198
10.3 Interactions Between Different Connexins	p. 199
10.4 Connexin Binding Proteins and Phosphorylation	p. 201
10.5 Channel Permeability and Signaling	p. 202
10.6 Connexins in Human Disease	p. 203
10.7 Role of Connexins in Vessel Inflammation and Atherosclerosis	p. 206
10.8 Conclusions	p. 207
References	p. 208
11 Tight Junctions in Simple and Stratified Epithelium	p. 217
11.1 Introduction	p. 217
11.2 Ultrastructure of Tight Junctions	p. 218
11.3 Tight Junctions and Epithelial Barrier Function	p. 219
11.3.1 Transmembrane Components	p. 219
11.3.2 Scaffolding Proteins	p. 221
11.3.3 Actin and Related Cytoskeleton Proteins	p. 221
11.4 Regulation of Tight Junction Barrier Function	p. 222
11.5 Tight Junctions and Epithelial Polarity	p. 222
11.5.1 Par3/Par6/aPKC Complex	p. 223
11.5.2 Crbs/Patj/Pals	p. 223
11.5.3 Fence Function	p. 224
11.6 Signaling from Tight Junctions: Coupling Junction Maturation to Transcription-Mediated Differentiation	p. 225
11.7 Tight Junctions in Stratifying Epithelia	p. 225
11.8 Tight Junctions and Disease	p. 227
11.9 Concluding Remarks	p. 228
Acknowledgments	p. 229
References	p. 229
12 Desmosomes in Development and Disease	p. 235
12.1 Introduction	p. 235
12.2 Molecular Composition of Desmosomes, Disease Associations, and Animal Models	p. 236
12.2.1 Desmosomal Cadherins	p. 236
12.2.2 Desmoplakin	p. 240
12.3 Plakoglobin	p. 240
12.4 Plakophilins	p. 242
12.5 Accessory Desmosomal Proteins	p. 243
12.6 Desmosomal Proteins in Embryonic Development	p. 243
12.7 Concluding Remarks	p. 244
Acknowledgments	p. 245
References	p. 245
13 Cadherin Trafficking and Junction Dynamics	p. 251
13.1 Introduction	p. 251
13.2 Exocytosis and Polarized Sorting of Adherens Junction Proteins	p. 252
13.3 Endocytosis of Adherens Junction Proteins	p. 255
13.4 Catenin Regulation of Cadherin Endocytosis	p. 258
13.5 Rho GTPase Regulation of Cadherin Endocytosis	p. 261
13.6 Co-Regulation of Cadherin and Receptor Tyrosine Kinase Function by Endocytosis	p. 262
13.7 Conclusions	p. 264
Acknowledgments	p. 266
References	p. 266
Part 3 Cell-Matrix and Cell-Cell Crosstalk
14 Crosstalk Between Cell-Cell and Cell-Matrix Adhesion	p. 273
14.1 Introduction	p. 273
14.1.1 Coordinate Regulation of Cell-Cell and Cell-Matrix Adhesion	p. 273
14.1.2 Crosstalk Between Integrins and Cadherins	p. 274
14.2 Mechanisms of Integrin-Cadherin Crosstalk	p. 275
14.2.1 Extracellular Proteolysis	p. 275
14.2.2 Cross-Regulation of Gene Expression	p. 277
14.2.3 Changes in Intracellular Force Generation	p. 278
14.2.4 Integrin-Cadherin Associations at Sites of Cell Adhesion	p. 279
14.2.5 Intracellular Signal Transduction Pathways	p. 281
14.2.5.1 FAK: An Integrin Effector that Signals to Cadherins	p. 282
14.2.5.2 Fer: A Tyrosine Kinase that Translocates between Cadherins and Integrins	p. 282
14.2.5.3 Rap1: A Central Regulator of Integrin-Cadherin Crosstalk Pathways?	p. 283
14.2.5.4 The Epidermis as a Model for Investigating Cadherin-Integrin Crosstalk	p. 285
14.3 Future Prospects	p. 286
Acknowledgments	p. 287
References	p. 287
Index	p. 295

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