Protein Phosphatase-1
Binding Motifs

By Paulina Wakula
Acta Biomedica Lovaniensia, No. 354
January 2006
Leuven University Press
ISBN: 9058675211
124 pages, Illustrated, 6 ¼” x 9 ½”
$75.00 Paper Original

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Contents include:

Acknowledgement
Table of contents
Publications
Abbreviations
Chapter 1. Introduction
I. Protein SER/THR phosphatase-1
I.A. Reversible protein phosphorylation
I.B. The catalytic subunit of protein phosphatase-1
I.C. PP1 holoenzymes
I.D. PP1 interactors
II. Translation initiation in eukaryotes
II.A. Model of translation initiation
II.B. The eIF2 complex
II.C. eIF2ß
III. Control of translation initiation by phosphorylation
III.A. eIF2a phosphorylation
III.B. eIF4E phosphorylation
III.C. eIF4E-BP phosphorylation
III.D. eIF2Be phosphorylation
III.E. Additional PP1 regulatory subunits in ribosomal fractions
Chapter 2. Aims and strategies
Chapter 3. Materials and methods
I. Materials
I.A. Chemicals and reagents
I.B. Buffers
I.C. Antibodies and peptides
I.D. Plasmid construction and protein preparations
II. Methods
II.A. Biochemical techniques
II.B. Cell culture, cell lysis and protein synthesis measurements
Chapter 4. Results and discussions
I. Role of the RVXF-motif in binding to protein phosphatase-1
I.A. Degeneracy of RVXF-motif
I.B. Comparison the RVXF-motif with other PP1-binding motifs
I.C. Construction of a PP1-Inhibitor-1 fusion
I.D. Discussion
II. The eukaryotic initiation factor 2 beta as a novel interactor of PP1
II.A. Identification of eIF2ß as a putative interactor of PP1
II.B. Confirmation of eIF2ß-PP1 interaction
II.C. Mapping of eIF2ß-PP1 interaction sites
II.D. Functional analysis of the eIF2ß-PP1 interaction
II.E. Discussion
Chapter 5. General discussion and perspectives
I. Protein phosphatase-1 binding motifs
II. eIF2ß as a PP1 interactor
Summary
Samenvatting
References

Biochemistry / Medicine

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