Protein Phosphatase Protocols

1. Front Matter

   Pages i-xiii

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2. Prokaryotic Protein-Serine/Threonine Phosphatases

   • Peter J. Kennelly

   Pages 1-21

3. Protein Phosphatase Type 1 and Type 2A Assays

   • S. Derek Killilea, Qi Cheng, Zhi-Xin Wang

   Pages 23-33

4. Analyzing Gene Expression with the Use of Serine/Threonine Phosphatase Inhibitors

   • Axel H. Schönthal

   Pages 35-40

5. Inhibitor-1, a Regulator of Protein Phosphatase 1 Function

   • John H. Connor, Hai Quan, Carey Oliver, Shirish Shenolikar

   Pages 41-58

6. I1 PP2A and I2 PP2A

   • Mei Li, Zahi Damuni

   Pages 59-66

7. Control of PP1 Activity Through Phosphorylation by Cyclin-Dependent Kinases

   • Norbert Berndt

   Pages 67-77

8. Regulation of Neuronal PP1 and PP2A During Development

   • Elizabeth Collins, Alistair T. R. Sim

   Pages 79-102

9. PTPA Regulating PP2A as a Dual Specificity Phosphatase

   • Veerle Janssens, Christine Van Hoof, Wilfried Merlevede, Jozef Goris

   Pages 103-115

10. Microinjection and Immunological Methods in the Analysis of Type 1 and 2A Protein Phosphatases from Mammalian Cells

    • Patric Turowski, Ned J. C. Lamb

    Pages 117-136

11. Use of Immunocomplexed Substrate for Detecting PP1 Activity

    • John W. Ludlow, Deirdre A. Nelson, Nancy A. Krucher

    Pages 137-143

12. The Biochemical Identification and Characterization of New Species of Protein Phosphatase 1

    • Monique Beullens, Willy Stalmans, Mathieu Bollen

    Pages 145-155

13. The Relationship Between Insulin Signaling and Protein Phosphatase 1 Activation

    • Louis Ragolia, Najma Begum

    Pages 157-167

14. Analysis of the Isoforms of Protein Phosphatase 1 (PP1) Isoforms with Polyclonal Peptide Antibodies

    • Margherita Tognarini, Emma Villa-Moruzzi

    Pages 169-183

15. Expression of Mouse Protein Phosphatase 2C in Eschericia coli and COS 7 Cells

    • Takayasu Kobayashi, Kazuyuki Kusuda, Motoko Ohnishi, Naoki Chida, Shinri Tamura

    Pages 185-189

16. Expression of Functional Protein Phosphatase 1 Catalytic Subunit in E. coli

    • Mariam Dohadwala, Norbert Berndt

    Pages 191-199

17. Protein Phosphatase 2A and Protein Phosphatase X Genes in Arabidopsis thaliana

    • Gemma Pujol, Albert Ferrer, Joaquin Ariño

    Pages 201-212

18. Separation of Protein Phosphatase Type 2C Isozymes by Chromatography on Blue Sepharose

    • Susanne Klumpp, Dagmar Selke

    Pages 213-218

19. Chromatographic Isolation of PP2A from Limulus Lateral Eyes

    • Samuel C. Edwards, Travis B. Van Dyke, Timothy H. Van Dyke, David L. Brautigan

    Pages 219-234

20. Purification and Assay of the Ptc/Tpd1 Protein Phosphatase 2C from the Yeast Saccharomyces cerevisiae

    • Matthew K. Robinson, Eric M. Phizicky

    Pages 235-242

A major mechanism by which cells regulate protein function is to place phosphate groups on serine and threonine residues. Though the steady-state level of protein phosphorylation depends on the relative activities of both kinases and phosphatases, a much greater effort has previously gone into the study of the former that the latter . Today, however, there is an increasing appreciation for the role that protein phosphatases play in the dynamic p- cess of protein phosphorylation . To date, there are four major types of protein serine/threonine phosphatase catalytic subunits, designated protein phosphatase type 1, 2A, 2B, and 2C . Each has been identified by the techniques of protein chemistry and enzymology and can be distinguished from one another by their preference for specific substrates as well as their sensitivity to certain acti- tors and inhibitors . Protein Phosphatase Protocols has been assembled in response to the growing interest these enzymes are receiving . The goal of this compilation is to provide a "how-to" experimental guide to aid newcomers as well as s- soned veterans in their research endeavors, thus further contributing towards our ever increasing knowledge of serine/threonine phosphatases . What you have before you contains contributions by many of the current and emerging leaders in the field . To highlight just a few, these chapters c- tain step-by-step information on how to isolate novel phosphatases and re- latory subunits, assay for activity, and generate immunological reagents for both biochemical and biological characterization of these enzymes .

"I would highly recommend this volume for anyone wishing to develop or optimize Ser/Thr protein phosphatase assays and/or biochemical procedures in their laboratories."-The Quarterly Review of Biology

• University of Rochester Cencer Center, Rochester

  John W. Ludlow

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