Reversible Protein Phosphorylation in Cell Regulation

This book, published in association with the journal MOLECULAR AND CELLULAR BIOCHEMISTRY , is dedicated to Ed Krebs and Eddy Fischer in celebration of their 1992 Nobel Prize in Physiology and Medicine. Reversible protein phosphorylation is a research field pioneered and developed by Krebs and Fischer. This book contains short reviews and original research papers contributed by Krebs and Fischer's coworkers, both former and current.
The contents reflect the two-way interaction between protein phosphorylation and other biomedical research fields. The chapters are grouped into four sections. The first two deal with structure/function aspects of protein kinases and protein mechanisms. Unlike many other research fields, which undergo periods of intense activity and productivity followed by relative calm, the protein phosphorylation field enjoyed continued growth both in scope and intensity, and the pace of this growth has increased markedly in recent years. This volume will provide a glimpse of the dynamism and diversity of the research activity representative of the current state of the field.

Texte du rabat

2 During our formative years with Dr. Krebs at Davis, ed until the ER becomes substantially depleted of Ca +. California, we (c. and M. Brostrom) were imbued with For example, acute exposure of GH3 pituitary cells to 2 2 our continuing interest in the roles of Ca+ and cAMP in Ca+ ionophore A23187 or EGTA has been found to re biological control mechanisms. We remember our time sult in the inhibition of amino acid incorporation. disap with Dr. Krebs with great affection both for his intense pearance of polysomal content with accumulation of interest and high standards in science and for his great monosomes and ribosomal subunits. sharp reduction of decency in the treatment of postdoctoral fellows. We the cellular content of 43S pre initiation complex. and have subsequently aspired, within the constraints of our the phosphorylation of elF-2ex and inhibition of eIF-2B ability, to pattern our behavior in accord with this expe [15-17]. Neither translational elongation nor peptide rience. Our current research involving the control of chain termination appeared to be affected in these ex protein synthesis at mRNA translation embodies much periments, since average ribosomal transit times and the methionylation of tRNA;met were not altered. Amino of the familiar in protein phosphorylation with some new twists that we shall highlight in this article with our acid incorporation was unaffected during the period of 2 associate. Dr. Prostko. Ca+ release prior to suppression of initiation.

Contenu
R.L. Khandelwal and J.H. Wang: Preface.- Protein Kinases.- Expression, purification, characterization, and deletion mutations of phosphorylase kinase ? subunit: identification of an inhibitory domain in the ? subunit.- Interaction sites on phosphorylase kinase for calmodulin.- Preparation and functional characterization of a catalytically active fragment of phosphorylase kinase.- Development and characterization of fluorescently-labeled myosin light chain kinase calmodulin-binding domain peptides.- Autophosphorylation: a salient feature of protein kinases.- Expression of cGMP-dependent protein kinase in Escherichia coli.- Chicken smooth muscle myosin light chain kinase is acetylated on its NH2-terminal methionine.- Calcium/calmodulin-dependent protein kinase II: role in learning and memory.- In vitro substrate specificity of protein tyrosine kinases.- Protein Phosphatases.- Mutagenesis of the catalytic subunit of rabbit muscle protein phosphatase-.- Serine phosphorylation of protein tyrosine phosphatase (PTP1B) in HeLa cells in response to analogues of cAMP or diacylglycerol plus okadaic acid.- Purification and characterization of the human protein tyrosine phosphatase, PTP ?, from a baculovirus expression system.- Protein tyrosine phosphatase activity in Leishmania donovani.- Protein Phosphorylation in Signal Transduction.- The phosphorylation of stathmin by MAP kinase.- Networking with mitogen-activated protein kinases.- Interleukin-8 activates microtubule-associated protein 2 kinase (ERK1) in human neutrophils.- Signal transduction through the cAMP-dependent protein kinase.- Casein kinase II in signal transduction and cell cycle regulation.- The MAP kinase cascade. Discovery of a new signal transduction pathway.- Does the insulin-mimetic action of vanadate involveinsulin receptor kinase?.- Cellular Regulation by Reversible Phosphorylation.- Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains.- Phosphorylation of myosin light chain kinase: a cellular mechanism for Ca2+ desensitization.- The role of protein phosphorylation in the regulation of cyclic nucleotide phosphodiesterases.- Reversible phosphorylation of eukaryotic initiation factor 2? in response to endoplasmic reticular signaling.- On the importance of protein phosphorylation in cell cycle control.- Evidence for an extra-cellular function for protein kinase A.- In situ regulation of cell-cell communication by the cAMP-dependent protein kinase and protein kinase C.- A-Kinase Anchoring Proteins: a key to selective activation of cAMP-responsive events?.