Guidebook to the Small GTPases

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Overview


In the last few years, the functional divergence of GTPases has attracted the attention of many researchers in structural biology, cell biology, cell growth and differentiation and developmental biology. Numerous studies have contributed important data on the biochemical features, intracellular localization, and functions of these proteins. This book is a summation of the information compiled so far on this family of proteins. An opening section introduces the different subfamilies and the structural features of their various members. The following chapters focus on the individual GTPases, their regulatory components and effector proteins. Intended to serve as an easy-to-use reference, this guidebook will be valued equally by experienced researchers and investigators beginning work in this expanding field.
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Editorial Reviews

From the Publisher

"The breadth and depth of knowledge contained in this guidebook as well as the accessibility of information make it an excellent addition to the other guidebooks in this series." --Journal of the American Chemical Society

"A thorough survey of the identities and cellular functions of small GTPases and their regulators....Highly recommended."--Quarterly Review of Biology

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Product Details

  • ISBN-13: 9780198599449
  • Publisher: A Sambrook and Tooze Publication at Oxford University Press
  • Publication date: 2/1/1996
  • Series: Guidebook Series
  • Pages: 498
  • Product dimensions: 7.50 (w) x 9.63 (h) x 1.10 (d)

Meet the Author

European Molecular Biology Laboratory, Heidelberg

University of Geneva

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Table of Contents

List of contributors
List of abbrevations
Part 1. Overview of the Ras superfamily of small GTPases
1. General introduction, Alan Hall and Marino Zerial
2. The Ras superfamily, Alfonso Valencia and Chris Sander
3. Three-dimensional structure of Ras and Ras-related proteins, Alfred Wittinghofer and Alfonso Valencia
4. Molecular cloning of Ras-related proteins, Armand Tavitian
5. GTP-binding proteins in plants, Nancy Terryn, Marc Van Montagu, and Dirk Inzé
6. The mammalian two-dimensional gel map of small GTP-binding proteins, Lukas A. Huber
7. CAXX farnesyl transferase, Miguel C. Seabra, Michael S. Brown, and Joseph L. Goldstein
8. CAXX geranylgeranyl transferase, Miguel C. Seabra, Joseph L. Goldstein, and Michael S. Brown
9. Rab geranylgeranyl transferase, Miguel C. Seabra, Michael S. Brown, and Joseph L. Goldstein
10. Rab escort proteins (REP1 and REP2), Miguel C. Seabra, Joseph L. Goldstein, and Michael S. Brown
11. Ram2p, Fuyuhiko Tamanoi
12. Dpr1/Ram1p, Fuyuhiko
13. Cal1/Cdc43p, Yoshikazu Ohya, Yasuhiro Anraku, and Cynthia E. Trueblood
14. Bet4p, Susan Ferro-Novick
15. Bet2p, Susan Ferro-Novick
Part 2. The Ras Subfamily
16. The Ras/Raf/ERK pathway, Chris Marshall
17. H-Ras, Frank McCormick
18. K-Ras, Frank McCormick
19. N-Ras, Frank McCormick
20. R-Ras, Maria Jose Fernandez-Sarabia and James R. Bischoff
21. TC21/R-Ras2, Suzanne M. Graham, Channing J. Der, Adrienne D. Cox, George T. Drivas, Mark G. Rush, and Peter D'Eustachio
22. RalsA, Pierre Chardin
23. RalB, Pierre Chardin
24. Rap1a and Rap1b, Véronique Pizon
25. Rap2a, Scott N. Peterson and Eduardo G. Lapetina
26. Rap2b, Scott N. Peterson and Eduardo G. Lapetina
27. Dras2, John G. Bishop III and Victor G. Corces
28. Let-60 Ras, Paul W. Sternberg and Min Han
29. Dictyostelium ras genes, Juliet Daniel, Gerald Weeks, and George B. Spiegelman
30. RasD, Sharon A. Louis, Gerald Weeks, and George B. Spiegelman
31. Sevenless, Marek Mlodzik
32. Drk, J. Paul Olivier and Tony Pawson
33. GRB2, Julian Downward
34. Shc, Giuliana Pelicci, Luisa Lanfrancone, and Pier Giuseppe Pelicci
35. Sos, Julian Downward
36. Ras-GRF, Larry A. Fieg
37. Cdc25]M]m (Dpd-GEF), Enzo Martegani, Marco Vanoni, Renata Zippel, Emmapaola Sturani and Lilia Alberghina
38. Smg-GDS, Kozo Kaibuchi and Yoshimi Takai
39. Vav, Amnon Altman and Erich Gulbins
40. Ral-GDS, Barton W. Giddings
41. p120-GAP, Frank McCormick
42. Neurofibromin, Frank McCormick
43. Rap-GAP, Frank McCormick
44. Dm Gap1, Ulrike Gaul
45. Kenneth W. Wood
46. MAP kinase activators: Mek1, Mek2, Sally Leevers and Chris Marshall
47. Extracellular signal-regulated kinases (ERKs), Sally Leevers and Chris Marshall
48. Rsk, Rey-Huei Chen
49. p62, Frank McCormick
50. Bcl2, James R. Bischoff and Maria Jose Fernandez-Sarabia
51. Ras1p, Ottavio Fasano
52. Ras2p, Ottavio Fasano
53. Rsr1p, Alan Bender and John R. Pringle
54. Cdc25p, Scott Powers
55. Sdc25p, Emmanuelle Boy-Marcotte and Michel Jacquet
56. Msi2p/Lte1p, Masaki Shirayama, Yasushi Matsui, Akio Toh-e, and Kazuma Tanaka
57. Bud5p, John Chant and John R. Pringle
58. Ira1p, Scott Powers
59. Ira2p, Scott Powers
60. Bud2p, Hay-Oak Park and John S. Chant
61. Sp-Ras, Yoshito Kaziro
62. Ste6, David A. Hughes and Masayuki Yamamoto
Part 3. The Rho Subfamily
63. The Rho subfamily of small GTPases, Alan Hall
64. Rho of Aplysia californica, Pascal Madaule
65. RhoA, Alan Hall
66. RhoB, Alan Hall
67. RhoC, Alan Hall
68. RhoD, Robert G. Parton and Martin Zerial
69. RhoG, Philippe Fort
70. Rac2, Gary M. Bokoch
71. Cdc42Hs, Richard Cerione
72. Rho-GDI, Kazuma Tanaka, Akira Kikuchi, Kozo Kaibuchi, Takuya Sasaki and Yoshimi Takai
73. Dbl, Richard Cerione
74. Rho-GAP, Alan Hall
75. p190, Jeffrey Settleman
76. The chimaerin and Bcr families, Louis Lim, Christine Hall, Thomas Leung, and Edward Manser
77. Rotund Rac-GAP, Annabel Guichard, Evelyne Bergeret, and Ruth Grffin-Shea
78. Rho-p21-associated protein kinases, Edward Manser, Thomas Leung, and Louis Lim
79. Rho1p, Pascal Madaule, Joni Johnson, Mary McCaffrey, Patrice Boquet, and Alan Myers
80. Rho2p, Pascal Madaule and Alan Myers
81. Rho3p, Yasushi Matsui, Jun Imai, and Akio Toh-e
82. Rho4p, Yasushi Matsui and Akio Toh-e
83. Cdc42p, Douglas L. Johnson and John R. Pringle
84. Cdc24p, Alan Bender and John R. Pringle
Part 4. The Rab subfamily
85. Rab Proteins, Marino Zerial
86. Rab1a, b, William E. Balch
87. Rab2, William E. Balch
88. Rab3a, Akira Kikuchi and Yoshima Takai
89. Rab3b, Akira Kikuchi and Yoshima Takai
90. Rab3c, Akira Kikuchi and Yoshima Takai
91. Rab3d, Philipp E. Scherer, Giulia Baldini, and Harvey F. Lodish
92. Rab4a, Ira Mellman
93. Rab4b, Cecilia Bucci and Marino Zerial
94. Rab5a, Marino Zerial
95. Rab5b and Rab5c, Cecilia Bucci, Anne Lütcke, Paul Dupree, and Marino Zerial
96. Rab6, Bruno Goud
97. Rab7
98. Rab8, Lukas A. Huber
99. Rab9, Suzanne R. Pfeffer
100. Rab10, Lukas A. Huber
101. Rab11, Sylvie Urbé and Robert G. Parton
102. Rab12, Lisa A. Elferink and Richard H. Schellers
103. Rab13, Lisa A. Elferink and Richard H. Schellers
104. Rab14, Lisa A. Elferink and Richard H. Schellers
105. Rab15, Lisa A. Elferink and Richard H. Schellers
106. Rab16, Lisa A. Elferink and Richard H. Schellers
107. Rab17, Anne Lütcke, Eero Lehtonen, and Marino Zerial
108. Rab18, Anne Lütcke and Marino Zerial
109. Rab19, Anne Lütcke and Marino Zerial
110. Rab20, Anne Lütcke and Marino Zerial
111. Rab21, Philippe Chavrier
112. Rab22, Vesa M. Olkkonen
113. Rab23, Vesa M. Olkkonen
114. Rab24, Vesa M. Olkkonen
115. Rab25, James R. Goldenring
116. Rab-GDI, Takuya Sasaki, Akira Kikuchi, Kozo Kaibuchi, and Yoshimi Takai
117. Rab-GDI2, Assia Shisheva and Michael P. Czech
118. Mss4, Janel Burton and Pietro DeCamilli
119. Rabphilin-3A, Hiromichi Shirataki, Kozo Kaibuchi, and Yoshimi Takai
120. Dictyastelium discoideum Rab- and Rho-related proteins, John Bush and James Cardelli
121. Ypt1p (Saccharomyces cerevisiae), Dieter Gallwitz
122. Sec4p, Peter Novick
123. Ypt51p, Birgit Singer-Krüger
124. Ypt52p, Birgit Singer-Krüger
125. Ypt53p, Birgit Singer-Krüger
126. Ypt6p, Ludger Hengst, Reiner Grabowski and Dieter Gallwitz
127. Ypt7p, Dietrich Scheglmann and Dieter Gallwitz
128. Gdi1p/Sec19p, Michelle D. Garrett and Peter Novick
129. Dss4p, Denise Roberts and Peter Novick
130. Gyp6p (Ypt6-GAP), Molly Strom, Petra Vollmer and Dieter Gallwitz
131. Bet1p/Sly12p, Susan Ferro-Novick
132. Sly1p, Hans Dieter Schmitt, Christiane Dascher and Dieter Gallwitz
133. Sly2p/Sec22p, Hans Dieter Schmitt, Rainer Ossig and Dieter Gallwitz
134. Sec22p, Susan Ferro-Novick
135. Ypt1 (Schizosaccharomyces pombe), John Armstrong
136. Ypt2, Maren Mundt and Dieter Gallwitz
137. Ypt5 (Schizosaccharomyces pombe), John Armstrong
138. Ryh1, Ludger Hengst and Dieter Gallwitz
Part 5. The Arf and Sar subfamilies
139. The ARF subfamily, Richard A. Kahn
140. Arf1, Richard A. Kahn
141. Arf2, Richard A. Kahn
142. Arf3, Richard A. Kahn
143. Arf4, Richard A. Kahn
144. Arf5, Richard A. Kahn
145. Arf6, Richard A. Kahn
146. Arl1, Richard A. Kahn
147. Arl2, Richard A. Kahn
148. Arl3, Richard A. Kahn
149. Sar1p, Charles Barlowe, Randy Schekman and Aki Nakano
150. Sec12p, Charles Barlowe and Randy Schekman
151. Sec23p, Tohru Yoshihisa, Charles Barlowe and Randy Schekman
Part 6. The Ran Family
152. Ran/TC4, F. Ralf Bischoff, Elias Coutavas, Peter D'Eustachio, Herwig Ponstingl, Mindong Ren and Mark Rush
153. RCC1, F. Ralf Bischoff, Takeharu Nishimoto and Herwig Ponstingl
154. TC4/Ran (Dictostelium disoideum), John Bush and James Cardelli
Organelle index
Subject index

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