International Review of Cell and Molecular Biology

 
 
Academic Press
  • 1. Auflage
  • |
  • erschienen am 30. Januar 2016
  • |
  • 418 Seiten
 
E-Book | ePUB mit Adobe DRM | Systemvoraussetzungen
E-Book | PDF mit Adobe DRM | Systemvoraussetzungen
978-0-12-805225-9 (ISBN)
 

International Review of Cell and Molecular Biology presents comprehensive reviews and current advances in cell and molecular biology, and includes articles that address the structure and control of gene expression, nucleocytoplasmic interactions, control of cell development and differentiation, and cell transformation and growth.

The series has a worldwide readership, maintaining a high standard by publishing invited articles on important and timely topics authored by prominent cell and molecular biologists.


  • Provides comprehensive reviews and current advances
  • Presents a wide range of perspectives on specific subjects
  • Valuable reference material for advanced undergraduates, graduate students, and professional scientists
1937-6448
  • Englisch
  • San Diego
  • |
  • USA
Elsevier Science
  • 20,14 MB
978-0-12-805225-9 (9780128052259)
0128052252 (0128052252)
weitere Ausgaben werden ermittelt
  • Cover
  • Title page
  • Copyright
  • Contents
  • Contributors
  • Chapter One - New Insights into Mechanisms and Functions of Nuclear Size Regulation
  • Abstract
  • 1 Introduction
  • 2 Overview of Cellular Structures and Activities that Contribute to Nuclear Size Determination
  • 2.1 Nuclear Structure and Models of Organelle Size Control
  • 2.2 Genome Size and Ploidy
  • 2.3 Chromatin State
  • 2.4 Cell Size and Nucleocytoplasmic Ratio
  • 2.5 Nucleocytoplasmic Transport
  • 2.6 Intranuclear Structures
  • 2.7 Extranuclear Structures
  • 2.8 Cell-Cycle Effects
  • 2.9 Signaling Pathways
  • 3 Model Systems to Elucidate Mechanisms of Nuclear Size Regulation
  • 3.1 Tetrahymena thermophila
  • 3.2 Yeasts and Fungi
  • 3.3 Plants
  • 3.4 Caenorhabditis elegans
  • 3.5 Drosophila melanogaster
  • 3.6 Zebrafish
  • 3.7 Xenopus
  • 3.8 Mammalian Model Systems
  • 4 Functional Significance of Nuclear Size and?Morphology
  • 4.1 Chromosome Positioning, Chromatin Organization, and Gene Expression
  • 4.2 Nuclear Mechanics and Cell Migration
  • 4.3 Nuclear Size and Morphology Changes in Cancer
  • 4.4 Nuclear Envelopathies
  • 5 Conclusions
  • Acknowledgments
  • References
  • Chapter Two - Rho Signaling in Dictyostelium discoideum
  • Abstract
  • 1 Introduction
  • 2 D. discoideum Rho GTPases
  • 2.1 Features and Expression
  • 2.2 Subcellular Localization
  • 2.3 Functional Studies
  • 2.3.1 Effects on Actin Cytoskeleton
  • 2.3.2 Rac1
  • 2.3.2.1 Subcellular Localization of Rac1
  • 2.3.2.2 Functional Studies on Rac1
  • 2.3.3 RacB
  • 2.3.4 RacC
  • 2.3.5 RacE
  • 2.3.5.1 RacE and Cytokinesis
  • 2.3.5.2 RacE and Chemotaxis
  • 2.3.6 RacF
  • 2.3.7 RacG
  • 2.3.8 RacH
  • 2.3.9 RacA, A RhoBTB Protein
  • 3 Effectors
  • 3.1 WASP Family
  • 3.1.1 WASP
  • 3.1.2 WASP-B
  • 3.1.3 Scar Complex
  • 3.1.3.1 Composition and Regulation of the Scar Complex
  • 3.1.3.2 Subcellular Localization and Functional Studies
  • 3.1.3.3 The Scar Complex and Cytokinesis
  • 3.1.3.4 The Scar Complex and Vesicle Trafficking
  • 3.2 P21-Activated Kinases
  • 3.2.1 PakA and PakB
  • 3.2.1.1 PakA
  • 3.2.1.2 PakB
  • 3.2.1.3 PakA and PakB in Endocytosis
  • 3.2.2 PakC
  • 3.2.3 PakD
  • 3.3 Coronin A
  • 3.4 Formins
  • 3.4.1 ForC
  • 3.4.2 ForF
  • 3.4.3 ForH
  • 3.5 IQGAP-Related Proteins and Filamin
  • 3.5.1 IQGAPs in Cell Division
  • 3.5.2 IQGAPs in Chemotaxis and Development
  • 3.6 F-BAR Family
  • 3.7 Other Effectors
  • 4 Guanine Nucleotide Dissociation Inhibitors
  • 4.1 Features of D. discoideum RhoGDIs
  • 4.2 Functional Studies on RhoGDI
  • 5 Guanine Nucleotide Exchange Factors
  • 5.1 Conventional RhoGEFs
  • 5.1.1 Myosin M
  • 5.1.2 RacGEF1
  • 5.1.3 GxcC
  • 5.1.4 GxcT
  • 5.1.5 GxcDD
  • 5.1.6 Roco Family RhoGEFs
  • 5.1.7 Other Conventional RhoGEFs
  • 5.2 The CZH Family of RhoGEFs and Elmo
  • 5.2.1 Dock and Zizimin
  • 5.2.2 Elmo
  • 6 GTPase Activating Proteins
  • 6.1 Dd5P4
  • 6.2 MEGAPs
  • 6.3 Other RhoGAPs
  • 7 Proteins With RhoGEF and RhoGAP Domains
  • 8 Processes Regulated by Rho GTPases in D. discoideum
  • 8.1 Rho Signaling and Chemotaxis to cAMP
  • 8.1.1 Rho Signaling at the Leading Front
  • 8.1.2 Rho Signaling at the Rear
  • 8.2 Rho Signaling and Vesicle Trafficking
  • 8.2.1 Phagocytosis and Macropinocytosis
  • 8.2.1.1 Rho Signaling During the Uptake Phase
  • 8.2.1.2 Rho Signaling During Transit and Exocytosis
  • 8.2.2 Other Vesicle Trafficking Processes
  • 8.3 Rho Signaling and Cytokinesis
  • 9 Concluding Remarks
  • Acknowledgments
  • References
  • Chapter Three- Building Blocks of Functioning Brain: Cytoskeletal Dynamics in Neuronal Development
  • Abstract
  • 1 Introduction
  • 2 Cytoskeletal dynamics and organization during neuronal development
  • 2.1 Actin-Binding Proteins
  • 2.1.1 Actin-Nucleating Proteins
  • 2.1.1.1 Arp2/3 and Nucleation Promoting Factors
  • 2.1.1.2 Cordon-Bleu
  • 2.1.1.3 Formins
  • 2.1.1.3.1 Diaphanous Formins
  • 2.1.2 Barbed-End Binding Proteins
  • 2.1.2.1 Ena/VASP Protein Family
  • 2.1.2.2 Lamellipodin
  • 2.1.3 Actin-Monomer Binding Proteins
  • 2.1.3.1 Profilin
  • 2.1.4 Actin-Bundling Proteins
  • 2.1.4.1 Fascin
  • 2.1.4.2 CRP1
  • 2.1.4.3 Palladin
  • 2.1.5 F-Actin-Severing Proteins
  • 2.1.5.1 ADF/Cofilin
  • 2.1.6 Other F-Actin-Binding Proteins
  • 2.1.6.1 Tropomodulin
  • 2.1.6.2 Tropomyosins
  • 2.1.6.3 UNC-115/abLIM Proteins
  • 2.1.7 F-Actin Motor Proteins
  • 2.1.7.1 Myosin II
  • 2.1.8 Membrane-Actin Linker Proteins
  • 2.1.8.1 Spectrin
  • 2.1.8.2 Ankyrin
  • 2.1.8.3 ERM Proteins
  • 2.1.8.4 Shootin1
  • 2.1.8.5 Af-6/Afadin
  • 2.2 MT-Binding Proteins
  • 2.2.1 MT-Stabilizing Proteins
  • 2.2.1.1 MAPs
  • 2.2.1.2 MAP2
  • 2.2.1.3 Tau
  • 2.2.1.4 MAP1B
  • 2.2.1.5 MAP1A
  • 2.2.1.6 Doublecortin
  • 2.2.1.7 Collapsin Response Mediator Proteins
  • 2.2.2 Plus-End Tracking Proteins
  • 2.2.2.1 End-Binding Proteins, EB1 and EB3
  • 2.2.2.2 Cytoplasmic Linker Proteins CLIP-170 and CLIP-115
  • 2.2.2.3 Cytoplasmic Linker Associated Protein
  • 2.2.2.4 Adenomatous Polyposis Coli
  • 2.2.2.5 Transforming Acidic Coiled-Coil Domain Family
  • 2.2.3 MT-Severing Protein
  • 2.2.3.1 Katanin
  • 2.2.3.2 Spastin
  • 2.2.4 MT-Destabilizing Proteins
  • 2.2.4.1 Stathmin
  • 2.2.4.2 SCG-10
  • 2.2.4.3 SCG-10-Like Protein
  • 2.2.4.4 Capzb2
  • 2.2.5 MT-Motor Proteins
  • 2.2.5.1 Kinesins
  • 2.2.5.2 Dynein and Dynein-Associated Proteins
  • 2.3 Actin/MT-Linking Actin-Binding Proteins
  • 2.3.1 Drebrin
  • 2.3.2 TcTex-1
  • 2.3.3 Pod1
  • 2.3.4 IQGAP1
  • 2.4 Molecular Switches: Rho GTPases and Their Downstream Effectors
  • 3 Concluding remarks
  • Acknowledgments
  • References
  • Chapter Four - Membrane Trafficking in Neuronal Development: Ins and Outs of Neural Connectivity
  • Abstract
  • 1 Introduction
  • 1.1 Neuronal Development
  • 1.2 Membrane Trafficking and Neuronal Development
  • 2 Exocytosis
  • 2.1 Exocytic SNARE Proteins
  • 2.1.1 V-SNAREs: VAMP-2 and VAMP-7
  • 2.1.2 SNAP Family of t-SNAREs
  • 2.1.2.1 SNAP25
  • 2.1.2.2 SNAP29
  • 2.1.2.3 SNAP47
  • 2.1.3 Syntaxins
  • 2.1.4 Regulators of SNARE Complex
  • 2.1.4.1 Munc Proteins
  • 2.1.4.2 TRIM9
  • 2.2 Vesicle Tethering Proteins
  • 2.2.1 LGL Family Proteins
  • 2.2.2 Exocyst Complex
  • 3 Endocytosis
  • 3.1 Receptor Endocytosis in Neurite Outgrowth
  • 3.2 Compartmentalization of Neuronal Endosomes
  • 4 ER and Golgi
  • 4.1 ER and Golgi Outposts
  • 4.2 R-SNARE Sec22
  • 5 Other Regulators of Membrane Traffic
  • 6 Conclusion and Future Directions
  • Acknowledgments
  • References
  • Chapter Five - Leukocytes Crossing the Endothelium: A Matter of Communication
  • Abstract
  • 1 Introduction
  • 2 Rolling and Adhesion: Leukocyte Perspective
  • 2.1 Tethering and Rolling: PSGL-1, L-Selectin, CD44
  • 2.1.1 PSGL-1
  • 2.1.2 L-Selectin
  • 2.1.3 CD44
  • 2.2 Firm Adhesion: Integrins LFA-1, Mac-1, VLA-4
  • 2.2.1 LFA-1
  • 2.2.2 Mac-1
  • 2.2.3 VLA-4
  • 3 Rolling and Adhesion: endothelial-cell Perspective
  • 3.1 Tethering and Rolling: P-selectin, E-selectin
  • 3.1.1 P-Selectin
  • 3.1.2 E-Selectin
  • 3.2 Firm Adhesion: ICAM-1, VCAM-1
  • 3.2.1 ICAM-1 and VCAM-1 Expression
  • 3.2.2 ICAM-1 and VCAM-1 Engagement
  • 3.2.3 ICAM-1 and VCAM-1 Recruitment
  • 3.2.4 Actin Adapter Proteins and Actin Cytoskeleton
  • 3.2.4.1 ERM Proteins
  • 3.2.4.2 a-Actinin-1 and -4
  • 3.2.4.3 Cortactin
  • 3.2.4.4 Filamin A and B
  • 3.2.4.5 Actin Adapter Proteins and Endothelial Stiffness
  • 3.2.4.6 Endothelial Docking Structure
  • 4 Diapedesis: Endothelial Cell-Cell Junction Regulation
  • 4.1 Tight Junctions
  • 4.2 PECAM-1 and CD99
  • 4.3 VE-Cadherin
  • 4.4 Regulation of Adherens Junctions
  • 4.4.1 Tyrosine Phosphorylation
  • 4.4.2 Tyrosine Phosphatases
  • 4.4.3 Serine Phosphorylation
  • 4.4.4 VE-Cadherin Internalization
  • 4.4.5 VE-Cadherin Shedding
  • 5 Hemodynamic Shear Forces During Leukocyte TEM
  • 5.1 Shear Flow as Prerequisite for TEM
  • 5.2 Sensing Shear Flow: Mechanotransduction Complex
  • 6 Concluding Remarks
  • References
  • Chapter Six - Membrane Dynamics and Signaling of the Coxsackievirus and Adenovirus Receptor
  • Abstract
  • 1 Introduction
  • 2 CAR Gene and Protein
  • 2.1 CAR Gene and Splice Variants
  • 2.2 CAR Protein and Posttranslational Modifications
  • 2.3 CAR Expression in Cells and Tissues
  • 2.4 Regulation of CAR Expression
  • 3 CAR Membrane Dynamics
  • 3.1 CAR Targeting to the Plasma Membrane
  • 3.2 CAR Endocytosis
  • 4 CAR Signaling and Role in Protein Trafficking
  • 4.1 Epithelial Cells
  • 4.2 The Heart
  • 4.3 The Brain
  • 4.4 Viral Infection
  • 4.5 Immunity
  • 4.6 Cancer Cells
  • 5 Concluding Remarks
  • References
  • Chapter Seven - Catecholaminergic System of Invertebrates: Comparative and Evolutionary Aspects in Comparison With the Octopaminergic System
  • Abstract
  • 1 Introduction
  • 2 "Protozoan" Protists
  • 3 Porifera
  • 4 Cnidaria and Ctenophora
  • 5 Protostomia
  • 5.1 Platyhelminthes
  • 5.2 Nemertea
  • 5.3 Mollusca
  • 5.4 Annelida
  • 5.5 Arthropoda
  • 5.6 Nematoda
  • 6 Deuterostomia
  • 6.1 Echinodermata
  • 6.2 Chordata
  • 7 Catecholamines During Development and Metamorphosis
  • 8 Concluding Remarks
  • Acknowledgments
  • References
  • Index
  • Back Cover

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