Small GTPases and Their Regulators, Part C: Proteins Involved in Transport: Volume 257
Published on 18. October 1995
Book
Hardback
360 pages
978-0-12-182158-6 (ISBN)
Description
General Description of the Volume:Small GTPases play a key role in many aspects of contemporary cell biology: control of cell growth and differentiation; regulation of cell adhesion and cell movement; the organization of the actin cytoskeleton; and the regulation of intracellular vesicular transport. This volume plus its companion Volumes 255 and 256 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.Volume 257 provides detailed protocols to effectively produce, modify, and assay for the function of small GTPases involved in vesicular traffic through the secretory pathway of eukaryotic cells.General Description of the Series:The critically acclaimed laboratory standard for more than forty 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.
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More details
Series
Language
English
Place of publication
San Diego
United States
Publishing group
Elsevier Science Publishing Co Inc
Target group
Professional and scholarly
Biochemists, molecular biologists, cell biologists, pharmacologists, neurophysiologists, and neurochemists.
Dimensions
Height: 229 mm
Width: 152 mm
Weight
670 gr
ISBN-13
978-0-12-182158-6 (9780121821586)
Copyright in bibliographic data and cover images is held by Nielsen Book Services Limited or by the publishers or by their respective licensors: all rights reserved.
Schweitzer Classification
Persons
Volume editor
The Scripps Research Institute, La Jolla, CA, USA
Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, USA
University College of London, U.K.
Editor-in-chief
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
Content
Expression, Purification, and Posttranslational Modification:
C. Nuoffer, F. Peter, and W.E. Balch, Purification of His6-Tagged Rab1 Proteins Using Bacterial and Insect Cell Expression Systems.
H. Horiuchi,O. Ullrich, C. Bucci, and M. Zerial, Purification of Posttranslationally Modified and Unmodified Rab5 Protein Expressed in Spodoptera frugiperda Cells.
M.A. Riederer, T. Soldati, A.B. Dirac-Svejstrup, and S.R. Pfeffer, Expression of Rab9 Protein in Escherichia coli: Purification and Isoprenylation in Vitro.
Y. Jiang, G. Rossi, and S. Ferro-Novick, Characterization of Yeast Type-II Geranylgeranyltransferase.
S.A. Armstrong, M.S. Brown, J.L. Goldstein, and M.C. Seabra, Preparation of Recombinant Rab Geranylgeranyltransferase and Rab Escort Proteins.
K. Kimura, T. Oka, and A. Nakano, Purification and Assay of Yeast Sar1p.
T. Rowe and W.E. Balch, Expression and Purification of Mammalian Sar1.
Guanine NucleotideExchange and Hydrolysis:
A. Kikuchi, H. Nakanishi, and Y. Takai, Purification and Properties of Rab3A.
T. Sasaki and Y. Takai, Purification and Properties of Bovine Rab-GDP Dissociation Inhibitor.
F. Peter, C. Nuoffer, I. Schalk, and W.E. Balch, Expression and Purification of Recombinant His6-Tagged Guanine Nucleotide Dissociation Inhibitor and Formation of Rab1 Complex.
D.M. Roberts, M.D. Garrett, and P.J. Novick, Purification of GDP Dissociation Stimulator Dss4 from Recombinant Bacteria.
J.L. Burton and P. De Camilli, Expression, Purification, and Functional Assay of Mss4.
C. Barlowe and R. Schekman, Expression, Purification, and Assay of Sec12p: A Sar1p-Specific GDP Dissociation Stimulator.
I.G. Macara and W.H. Brondyk, Oligonucleotide Mutagenesis of Rab GTPases.
P. Vollmer and D. Gallwitz, High Expression Cloning, Purification, and Assay of Ypt-GTPase Activating Proteins.
P.A. Randazzo, O. Weiss, and R.A. Kahn, Preparation of Recombinant ADP-Ribosylation Factor.
F.R. Bischoff and H. Ponstingl, Catalysis of Guanine Nucleotide Exchange of Ran by RCC1 and Stimulation of Hydrolysis of Ran-Bound GTP by Ran-GAP1.
T. Yeung, T. Yoshihisa, and R. Schekman, Purification of Sec23p-Sec24p Complex.
Cell Expression and Analysis in Vivo:
H. Stenmark, C. Bucci, and M. Zerial, Expression of Rab GTPase Using Recombinant Vaccinia Viruses.
C. Dascher, E.J. Tisdale, and W.E. Balch, Transient Expression of Small GTPases to Study Protein Transport along Secretory Pathway in Vivo Using the Recombinant T7 Vaccinia Virus System.
C. Dascher, J.K. VanSlyke, L. Thomas, W.E. Balch, and G. Thomas, Preparation of Recombinant Vaccinia Virus for Expression of Small GTPases.
L. Martin-Parras and M. Zerial, Using Oligonucleotides for Cloning Rab Proteins by PCR.
W.H. Brondyk and I.G. Macara, Use of Two-Hybrid System to Identify Rab-Binding Proteins.
H. Damke, M. Gossen, S. Freundlieb, H. Bujard, and S.L. Schmid, Tightly Regulated and Inducible Expression of Dominant Interfering Dynamin Mutant in Stably Transformed HeLa Cells.
R.W. Holz, R.A. Senter, and M.D. Uhler, Investigation by Transient Transfection of the Effects on Regulated Exocytosis of Rab3A.
M.D. Garrett and P.J. Novick, Expression, Purification, and Assays of Gdi1p from Recombinant Escherichia coli. Biological Activity:
O. Ullrich, H. Horiuchi, K. Alexandrov, and M. Zerial, Use of Rab-GDP Dissociation Inhibitor for Solubilization and Delivery of Rab Proteins to Biological Membranes in Streptolysin O-Permeabilized Cells.
T. Soldati, A.D. Shapiro, and S.R. Pfeffer, Reconstitution of Rab9 Endosomal Targeting and Nucleotide ExchangeUsing Purified Rab9-GDP Dissociation Inhibitor Complexes and Endosome-Enriched Membranes.
J.M. McCaffery and M.G. Farquhar, Localization of GTPases by Indirect Immunofluorescence and Immunoelectron Microscopy.
F. Melchior, D.J. Sweet, and L. Gerace, Analysis of Ran/Tc4 Function in Nuclear Protein Import.
H. Shirataki and Y. Takai, Purification and Properties of Rabphilin-3A.
L.A. Huber, P. Dupree, and C.G. Dotti, Use of Antisense Oligonucleotides to Study Rab Function in Vivo.
H.A. Brown and P.C. Sternweis, Stimulation of Phospholipase D by ADP-Ribosylation Factor.
C. Murphy and M. Zerial, Expression of Rab Proteins during Mouse Embryonic Development.
Author Index.
Subject Index.
C. Nuoffer, F. Peter, and W.E. Balch, Purification of His6-Tagged Rab1 Proteins Using Bacterial and Insect Cell Expression Systems.
H. Horiuchi,O. Ullrich, C. Bucci, and M. Zerial, Purification of Posttranslationally Modified and Unmodified Rab5 Protein Expressed in Spodoptera frugiperda Cells.
M.A. Riederer, T. Soldati, A.B. Dirac-Svejstrup, and S.R. Pfeffer, Expression of Rab9 Protein in Escherichia coli: Purification and Isoprenylation in Vitro.
Y. Jiang, G. Rossi, and S. Ferro-Novick, Characterization of Yeast Type-II Geranylgeranyltransferase.
S.A. Armstrong, M.S. Brown, J.L. Goldstein, and M.C. Seabra, Preparation of Recombinant Rab Geranylgeranyltransferase and Rab Escort Proteins.
K. Kimura, T. Oka, and A. Nakano, Purification and Assay of Yeast Sar1p.
T. Rowe and W.E. Balch, Expression and Purification of Mammalian Sar1.
Guanine NucleotideExchange and Hydrolysis:
A. Kikuchi, H. Nakanishi, and Y. Takai, Purification and Properties of Rab3A.
T. Sasaki and Y. Takai, Purification and Properties of Bovine Rab-GDP Dissociation Inhibitor.
F. Peter, C. Nuoffer, I. Schalk, and W.E. Balch, Expression and Purification of Recombinant His6-Tagged Guanine Nucleotide Dissociation Inhibitor and Formation of Rab1 Complex.
D.M. Roberts, M.D. Garrett, and P.J. Novick, Purification of GDP Dissociation Stimulator Dss4 from Recombinant Bacteria.
J.L. Burton and P. De Camilli, Expression, Purification, and Functional Assay of Mss4.
C. Barlowe and R. Schekman, Expression, Purification, and Assay of Sec12p: A Sar1p-Specific GDP Dissociation Stimulator.
I.G. Macara and W.H. Brondyk, Oligonucleotide Mutagenesis of Rab GTPases.
P. Vollmer and D. Gallwitz, High Expression Cloning, Purification, and Assay of Ypt-GTPase Activating Proteins.
P.A. Randazzo, O. Weiss, and R.A. Kahn, Preparation of Recombinant ADP-Ribosylation Factor.
F.R. Bischoff and H. Ponstingl, Catalysis of Guanine Nucleotide Exchange of Ran by RCC1 and Stimulation of Hydrolysis of Ran-Bound GTP by Ran-GAP1.
T. Yeung, T. Yoshihisa, and R. Schekman, Purification of Sec23p-Sec24p Complex.
Cell Expression and Analysis in Vivo:
H. Stenmark, C. Bucci, and M. Zerial, Expression of Rab GTPase Using Recombinant Vaccinia Viruses.
C. Dascher, E.J. Tisdale, and W.E. Balch, Transient Expression of Small GTPases to Study Protein Transport along Secretory Pathway in Vivo Using the Recombinant T7 Vaccinia Virus System.
C. Dascher, J.K. VanSlyke, L. Thomas, W.E. Balch, and G. Thomas, Preparation of Recombinant Vaccinia Virus for Expression of Small GTPases.
L. Martin-Parras and M. Zerial, Using Oligonucleotides for Cloning Rab Proteins by PCR.
W.H. Brondyk and I.G. Macara, Use of Two-Hybrid System to Identify Rab-Binding Proteins.
H. Damke, M. Gossen, S. Freundlieb, H. Bujard, and S.L. Schmid, Tightly Regulated and Inducible Expression of Dominant Interfering Dynamin Mutant in Stably Transformed HeLa Cells.
R.W. Holz, R.A. Senter, and M.D. Uhler, Investigation by Transient Transfection of the Effects on Regulated Exocytosis of Rab3A.
M.D. Garrett and P.J. Novick, Expression, Purification, and Assays of Gdi1p from Recombinant Escherichia coli. Biological Activity:
O. Ullrich, H. Horiuchi, K. Alexandrov, and M. Zerial, Use of Rab-GDP Dissociation Inhibitor for Solubilization and Delivery of Rab Proteins to Biological Membranes in Streptolysin O-Permeabilized Cells.
T. Soldati, A.D. Shapiro, and S.R. Pfeffer, Reconstitution of Rab9 Endosomal Targeting and Nucleotide ExchangeUsing Purified Rab9-GDP Dissociation Inhibitor Complexes and Endosome-Enriched Membranes.
J.M. McCaffery and M.G. Farquhar, Localization of GTPases by Indirect Immunofluorescence and Immunoelectron Microscopy.
F. Melchior, D.J. Sweet, and L. Gerace, Analysis of Ran/Tc4 Function in Nuclear Protein Import.
H. Shirataki and Y. Takai, Purification and Properties of Rabphilin-3A.
L.A. Huber, P. Dupree, and C.G. Dotti, Use of Antisense Oligonucleotides to Study Rab Function in Vivo.
H.A. Brown and P.C. Sternweis, Stimulation of Phospholipase D by ADP-Ribosylation Factor.
C. Murphy and M. Zerial, Expression of Rab Proteins during Mouse Embryonic Development.
Author Index.
Subject Index.