Hall Regulators and Effectors of Small GTPases, Part F: Ras Family I

1. Auflage 2001
ISBN: 978-0-08-052255-5
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band Volume 332, 492 Seiten, Web PDF

Reihe: Methods in Enzymology

The critically acclaimed laboratory standard for more than 40 years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today, truly an essential publication for researchers in all fields of life sciences.This volume and its companions (Volumes 255, 256, 257, and the forthcoming 325 and 329) cover all biochemical and biological assays currently in use for analyzing the role of small GTPases in these aspects of cell biology at the molecular level.

Autoren/Hrsg.

Hall, Alan

Inhaltsverzeichnis

1;Cover;1
2;Title Page;4
3;Copyright Page;5
4;Table of Contents;6
5;Contributors to Volume 332;10
6;Preface;14
7;Volumes in Series;16
8;Section I: Protein Expression and Protein–Protein Interactions;36
8.1;Chapter 1. Mammalian Expression Vectors for Ras Family Proteins: Generation and Use of Expression Constructs to Analyze Ras Family Function;38
8.2;Chapter 2. Protein Transduction: Delivery of Tat–GTPase Fusion Proteins into Mammalian Cells;71
8.3;Chapter 3. Green Fluorescent Protein-Tagged Ras Proteins for Intracellular Localization;85
8.4;Chapter 4. Targeting Proteins to Membranes, Using Signal Sequences for Lipid Modifications;99
8.5;Chapter 5. Targeting Proteins to Specific Cellular Compartments to Optimize Physiological Activity;112
8.6;Chapter 6. Mapping Protein–Protein Interactions with Alka- line Phosphatase Fusion Proteins;123
8.7;Chapter 7. Assays of Human Postprenylation Processing En- zymes;138
8.8;Chapter 8. In Vivo Prenylation Analysis of Ras and Rho Pro- teins;150
8.9;Chapter 9. Ras Interaction with RalGDS Effector Targets;162
8.10;Chapter 10. RAS Interaction with RIN1 Effector Target;174
8.11;Chapter 11. Ras and Rap1 Interaction with AF-6 Effector Target;186
9;Section II: Screening Analyses;204
9.1;Chapter 12. Analysis of Protein Kinase Specificity by Peptide Libraries and Prediction of in Vivo Substrates;206
9.2;Chapter 13. Peptide Library Screening for Determination of SH2 or Phosphotyrosine-Binding Domain Sequences;218
9.3;Chapter 14. Expression Cloning of Farnesylated Proteins;230
9.4;Chapter 15. Expression Cloning to Identify Monomeric GTP- Binding Proteins by GTP Overlay;238
9.5;Chapter 16. Retrovirus cDNA Expression Library Screening for Oncogenes;246
9.6;Chapter 17. Identification of Ras-Regulated Genes by Representational Difference Analysis;256
9.7;Chapter 18. Differential Display Analysis of Gene Expression Altered by ras Oncogene;268
9.8;Chapter 19. cDNA Array Analyses of K-Ras-Induced Gene Transcription;280
9.9;Chapter 20. Ras Signaling Pathway for Analysis of Protein–Protein Interactions;295
9.10;Chapter 21. Isolation of Effector-Selective Ras Mutants by Yeast Two-Hybrid Screening;305
9.11;Chapter 22. Two-Hybrid Dual Bait System to Discriminate Specificity of Protein Interactions in Small GTPases;312
9.12;Chapter 23. Functional Proteomics Analysis of GTPase Signal- ing Networks;335
10;Section III: Analyses of Mitogen-Activated Protein Kinase Cascades;352
10.1;Chapter 24. Analyzing JNK and p38 Mitogen-Activated Protein Kinase Activity;354
10.2;Chapter 25. Phospho-Specific Mitogen-Activated Protein Kinase Antibodies for ERK, JNK, and p38 Activation;372
10.3;Chapter 26. Immunostaining for Activated Extracellular Signal-Regulated Kinases in Cells and Tissues;378
10.4;Chapter 27. Dominant Negative Mutants of Mitogen-Activated Protein Kinase Pathway;388
10.5;Chapter 28. Scaffold Protein Regulation of Mitogen-Activated Protein Kinase Cascade;403
10.6;Chapter 29. Bacterial Expression of Activated Mitogen-Activated Protein Kinases;422
10.7;Chapter 30. Steroid Receptor Fusion Proteins for Conditional Activation of Raf–MEK–ERK Signaling Pathway;436
10.8;Chapter 31. Pharmacologic Inhibitors of MKK1 and MKK2;452
10.9;Chapter 32. Analysis of Pharmacologic Inhibitors of Jun N-Ter- minal Kinases;467
11;Author Index;488
12;Subject Index;512