Current Topics in Cellular Regulation

List of Contributors

Roles of Eukaryotic Initiation Factor 2 Ancillary Factors in the Regulation of Eukaryotic Protein Synthesis Initiation

I. Introduction

II. eIF-2

III. Co-eIF-2A

IV. Co-eIF-2B

V. Co-eIF-2C

VI. eIF-2 Kinases

VII. RF

VIII. A Proposed Mechanism for Regulation of the Early Steps in Peptide Chain Initiation in Reticulocyte Lysates by eIF-2 Ancillary Factors

IX. Concluding Remarks

References

The Role of Phosphorylation in the Regulation of Eukaryotic Initiation Factor 2 Activity

I. Introduction

II. Translational Control in Rabbit Reticulocyte Lysate

III. Phosphorylation State of eIF-2

IV. Is Ternary Complex Formation the Only Initiation Step Affected in Hemin-Deficient Lysate?

V. Other Modifications of eIF-2 Which Provide Insights into the Regulation of Its Activity

VI. Role of Phosphorylation in the Regulation of eIF-2 Activity

VII. Summary

References

Probing the Function of the Eukaryotic 5′-Cap Structure Using Monoclonal Antibodies to Cap-Binding Proteins

I. Introduction

II. Monoclonal Antibodies to Cap-Binding Proteins

III. Reaction of Monoclonal Antibodies with High-Molecular-Weight Proteins Antigenically Related to the 24-Cap-Binding Protein

IV. ATP-Mg2+-Dependent Cross-Linking of Cap-Binding Proteins to mRNA

V. Effect of Anti-Cap-Binding Protein Monoclonal Antibodies on Protein Synthesis

VI. Cap-Binding Proteins and the Cytoskeleton

VII. Summary

References

Criteria for Establishment of the Biological Significance of Ribosomal Protein Phosphorylation

I. Introduction

II. Methodology

III. Changes in Vivo

IV. Signaling Systems

V. Reconstruction in Vitro

References

Casein Kinases—Multipotential Protein Kinases

I. Introduction

II. Physicochemical Characterization

III. Substrate Specificity

IV. Comparison with Casein Kinases from Mammary Gland

V. Regulation

VI. Phosphorylation of Endogenous Proteins

VII. Criteria for Classification of Casein Kinases

VIII. Conclusions

References

Phosphoprotein Phosphatases

I. Introduction

II. Multiple Forms and Substrate Specificity of Phosphoprotein Phosphatases

III. Purification and Properties of the Mr = 35,000 Phosphoprotein Phosphatases

IV. Relationship Between Phosphoprotein Phosphatases and Alkaline Phosphatases

V. Heat-Stable Protein Effectors

VI. High-Molecular-Weight Forms of Type I Phosphoprotein Phosphatase

VII. Regulation of Phosphoprotein Phosphatases

VIII. Conclusion

References

Note Added in Proof

ADP-Ribosylation Reactions

I. Mono(ADP-Ribosyl)ation and Poly(ADP-Ribosyl)ation

II. Poly(ADP-Ribosyl)ation Reactions in Vitro

III. Poly(ADP-Ribosyl)ation and DNA Repair

IV. Conclusions

References

Commitment to Terminal Differentiation and the Cell Cycle

I. Introduction

II. Induced Commitment to Terminal Erythroid Differentiation

III. Characteristics of the Commitment Process

IV. Inducer Effects in Relation to the Cell Division Cycle

V. Relation of the Cell Cycle to the Replication of α- and β-Globin DNA Sequences in Erythroleukemia Cells

VI. Summary

References

The Turnover Characteristics of Lactate Dehydrogenase

I. Introduction

II. Methodological Considerations

III. Isozyme Turnover

IV. Physiological Variations

V. Biodegradation and Its Regulation

VI. Concluding Comments

References

The Role of Urea Synthesis in the Removal of Metabolic Bicarbonate and the Regulation of Blood pH

I. Introduction

II. The Problem: Need for Disposal of HCO3-

III. The Solution: Acquisition of Proton from NH4+

IV. The Role of the Kidney

V. Regulation

VI. Discussion

VII. Summary

VIII. Appendix A: Equations for Relevant Catabolic Reactions or Processes

IX. Appendix B: Necessity for Disposal of HCO3-

References

Index

Contents of Previous Volumes