Protein Prenylation, Part B

Protein Prenylation, Part B

1st Edition - November 8, 2011

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  • Editors: Christine Hrycyna, Martin Bergo, Fuyuhiko Tamanoi
  • Hardcover ISBN: 9780124159228
  • eBook ISBN: 9780124159648

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Description

This volume of The Enzymes features high-caliber thematic articles on the topic of glycosylphosphatidylinositol (GPI) anchoring of proteins.

Key Features

  • Contributions from leading authorities
  • Informs and updates on all the latest developments in the field

Readership

Biochemists, cell biologists, molecular biologists, biophysicists

Table of Contents

  • Preface

    The Enzymology of CAAX Protein Prenylation

    I. Abstract

    II. Introduction

    III. Protein FTase

    IV. Protein GGTase-I

    V. Conclusions

    Acknowledgments

    CAAX Processing and Yeast a-Factor Biogenesis

    I. Abstract

    II. Introduction

    III. The a-Factor Mating Pheromone of S. cerevisiae as an Early Prototype for Dissecting the CAAX-Processing Pathway

    IV. Biogenesis Pathway of a-Factor: Genetic and Biochemical Analysis of the a-Factor Machinery

    V. Progeria—The Role of Prenylation and ZMPSTE24 in Progeroid Disorders

    VI. A Prenylated, Secreted Molecule Involved in Drosophila Germ Cell Migration Requires a Pathway Strikingly Similar to That of a-Factor Biogenesis

    Acknowledgments

    Prenylation and Phosphorylation of Ras Superfamily Small GTPases

    I. Abstract

    II. Introduction

    III. Small GTPase Prenylation

    IV. C-Terminal Phosphorylation of Prenylated Ras Family Small GTPases

    V. C-Terminal Phosphorylation of Prenylated Rho Family Small GTPases

    VI. C-Terminal Phosphorylation of Prenylated Rab Family Small GTPases

    VII. Conclusions

    Acknowledgments

    Biochemical and Biological Functions of Isoprenylcysteine Carboxyl Methyltransferase

    I. Abstract

    II. Introduction

    III. Icmt: Structure and Biological Function

    IV. ICMT Substrate Specificity

    V. Effect of Methylation by Icmt on Substrate Function: In Vitro Studies

    VI. ICMT Effect on Substrate Function: In Vivo Studies

    VII. Conclusions

    Chemical Probes of Protein Prenylation

    I. Abstract

    II. Introduction

    III. Prenyl Analogs as FTase Inhibitors (FTIs)

    IV. Prenyl Analogs as Mechanistic and Structural Probes

    V. Substrate Specificity Studies

    VI. Prenyl Proteomics Studies

    VII. Future Directions

    Geranylgeranyltransferase-1 Inhibitors

    I. Abstract

    II. Introduction

    III. Biochemistry of Protein Prenylation

    IV. Validation of GGT-1 as a Target in a Genetic Mouse Model

    V. Design of CaaX Peptidomimetics as PTIs and Identification of PTIs from High-Throughput Screens (HTS)

    VI. FTIs as Anticancer Drugs

    VII. GGTI Effects in Cultured Cells and In Vivo

    VIII. GGTIs in the Clinic

    IX. The Use of PTIs in Other Diseases

    X. Future Directions and Challenges

    Acknowledgments

    Small-Molecule Inhibitors of GGTase-I from the Heterocycle Library Derived from Phosphine Catalysis

    I. Abstract

    II. Introduction

    III. Phosphine Catalysis-Based Chemical Compound Library and Identification of Initial GGTI Compounds P3-E5 and P5-H6

    IV. Cell Active Compound P61-A6

    V. Tumor Growth Inhibition by P61-A6

    VI. Long Plasma Half Life of P61-A6 and Pharmacokinetic Parameters

    VII. Identification of Dual Specificity Inhibitors of GGTase-I and RabGGTase

    VIII. Identification of Specific Inhibitors of RabGGTase from the Library

    IX. Conclusion and Future Prospects

    Acknowledgment

    Inhibition of Rab Prenylation

    I. Abstract

    II. Introduction

    III. RabGGTase Inhibitors

    IV. Summary and Outlook

    Inhibitors of Postprenylation CAAX Processing Enzymes

    I. Abstract

    II. Introduction

    III. Inhibitors of Rce1

    IV. Inhibitors of Icmt

    V. Conclusion

    The Ras Converting Enzyme (Rce1p)

    I. Abstract

    II. Introduction

    III. Identification of Rce1p and Its Orthologs

    IV. The Basis for Rce1p as a Therapeutic Target for Disease

    V. Rce1p and Ste24p Have Different Target Specificities

    VI. The Recognition of Specific CaaX Motifs is Influenced by Protein Context

    VII. Rce1p Influences the Localization of Some But Not All of Its Targets

    VIII. Rce1p Inhibitors Can Be Assay Independent and Assay Dependent

    IX. Structural Chemistry and Proposed Mechanism

    X. Conclusions and Future Directions

    Acknowledgments

    Cysmethynil, a Specific Small-Molecule Inhibitor of Isoprenylcysteine Carboxylmethyl Transferase (Icmt)

    I. Abstract

    II. Prenylation Process

    III. Rationale for Targeting Icmt

    IV. Icmt and Its Functional Importance in Biology

    V. Development of Icmt Inhibitors

    VI. Cysmethynil, a Nonstructure Analog Small-Molecule Inhibitor of Icmt

    VII. Inhibition of Icmt by Cysmethynil Induces Autophagy and Cell Death, Potential for Cancer Therapy

    VIII. Cysmethynil Inhibition of Icmt Results in Reduction of Rho-Mediated Cell Migration, Suggesting a Potential Role in Cancer Metastasis

    IX. Current and Future Work to Identify Better Icmt Inhibitors Through Medicinal Chemistry

    The Isoprenoid Biosynthetic Pathway and Statins

    I. Abstract

    II. The Isoprenoid Biosynthetic Pathway

    III. Statins

    IV. Statins and the IBP

    V. Future Directions

    Inhibition of Farnesyl and Geranylgeranyl Diphosphate Synthases

    I. Abstract

    II. The Isoprenoid Biosynthetic Pathway

    III. Nitrogenous Bisphosphonates

    IV. GGDPS Inhibitors

    V. Future Directions

Product details

  • No. of pages: 372
  • Language: English
  • Copyright: © Academic Press 2011
  • Published: November 8, 2011
  • Imprint: Academic Press
  • Hardcover ISBN: 9780124159228
  • eBook ISBN: 9780124159648

About the Serial Volume Editors

Christine Hrycyna

Affiliations and Expertise

Purdue University, West Lafayette, Indiana

Martin Bergo

Affiliations and Expertise

Wallenberg Laboratory, Institute of Medicine, Sahlgrenska Hospital, Gothenburg, Sweden

Fuyuhiko Tamanoi

Fuyu Tamanoi is a biochemist who has served on the UCLA School of Medicine and UCLA College faculty since he joined the Department of Microbiology, Immunology & Molecular Genetics in 1993. He became a full professor in 1997.

Affiliations and Expertise

Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, USA

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