Protein degradation. Volume 1, Ubiquitin and the chemistry of life
The first volume in a new series dedicated to protein degradation, this book lays the foundations of targeted protein breakdown via the ubiquitin pathway. The outstanding importance of the ubiquitin pathway has been recognized with the 2004 Nobel Prize in Chemistry for Aaaron Chiechanover, Avram Hershko, and Irwin Rose. Aaron Ciechanover is one of the editors of this series, and Avram Hershko has contributed to the opening chapter of the present volume. Drawing on the the expertise of two Nobel prize winners, this handy reference compiles information on the initial steps of the ubiquiti
Protein Degradation, v. 3
1 online resource (1 volume) : illustrations.
9783527605569, 9781280520624, 3527605568, 1280520620
68966600
Cover
Contents
Preface
List of Contributors
1 Brief History of Protein Degradation and the Ubiquitin System
146;1 Introductory Remarks
146;2 Protein Degradation 8211; Does It Exist63;
146;3 Discovery of the Role of Ubiquitin in Protein Degradation
146;4 Identification of Enzymes of the Ubiquitin45;mediated Proteolytic System
146;5 Discovery of Some Basic Cellular Functions of the Ubiquitin System
146;6 Concluding Remarks
References
2 N45;terminal Ubiquitination58; No Longer Such a Rare Modification
Abstract
246;1 Background
246;2 Results
246;3 Discussion
Acknowledgments
References
3 Evolutionary Origin of the Activation Step During Ubiquitin45;dependent Protein Degradation
Abbreviations
Abstract
346;1 Introduction
346;146;1 Activation of Ubiquitin and Ubiquitin45;like Proteins
346;146;2 Molybdenum Cofactor Biosynthesis
346;2 The Crystal Structure of MoaD Reveals the Ubiquitin Fold
346;3 Structural Studies of the MoeB8211;MoaD Complex
346;346;1 Structure of MoeB
346;346;2 The MoeB8211;MoaD Interface
346;346;3 Structure of MoeB8211;MoaD with Bound ATP
346;346;4 Structure of the MoaD Adenylate
346;346;5 Fate of the Adenylate
346;4 Structure of the NEDD8 Activator
346;446;1 Overall Structure of the NEDD845;E1
346;446;2 Comparison with the MoaD8211;MoeB Complex
346;446;3 Conformational Changes during the Formation of the Acyl Adenylate
Summary
Acknowledgments
References
4 RING Fingers and Relatives58; Determinators of Protein Fate
446;1 Introduction and Overview
446;146;1 Historical Perspective
446;2 RING Fingers as E3s
446;246;1 General Considerations
446;246;2 Structural Analysis and Structure8211;Function Relationships
446;246;3 Other Protein8211;Protein Interaction Motifs in RING finger Proteins
446;246;4 Variations on the RING Finger
446;246;5 High45;order Structure of RINGs 8211; TRIMs
446;3 RING Fingers in Cell Signaling
446;346;1 Siahs
446;346;2 IAPs
446;346;3 TRAFs
446;346;4 Cbls
446;4 Multi RING finger Proteins
446;446;1 Mindbomb and TRIADs
446;446;2 Parkin and Parkinson8217;s Disease
446;5 Regulation of p53 by Mdm2 and other RING finger Proteins
446;546;1 Mdm2
446;546;2 Pirh2
446;546;3 MdmX
446;546;4 Arf and Other Modulators of Mdm2 Activity
446;546;5 Other Potential Mdm2 Substrates
446;546;6 Mdm2 and Therapeutic Intervention in Cancer
446;6 Conclusion 8211; Perspective
Acknowledgments
References
5 Ubiquitin45;conjugating Enzymes
546;1 Introduction
546;2 Historical Background
546;3 What is an E263;
546;4 Functional Diversity of Ubiquitin45;conjugating Enzymes
546;446;1 Functions Related to Proteasome Proteolysis
546;446;2 Endocytosis and Trafficking
546;446;3 Non45;proteolytic Functions
546;446;4 E2s of Uncertain Function
546;446;5 E2 Enzymes and Disease