Protein phosphorylation / / edited by F. Marks

• Record Nr.: UNINA9910144009603321
• Pubbl/distr/stampa: Weinheim, [Germany] : , : VCH, , 1996; ©1996
• ISBN: 1-281-84268-0; 9786611842680; 3-527-61503-2; 3-527-61502-4
• Descrizione fisica: 1 online resource (409 p.)
• Disciplina: 572.65; 574.19245
• Soggetti: Phosphoproteins - Synthesis; Phosphoproteins - Metabolism; Protein kinases; Electronic books.
• Lingua di pubblicazione: Tedesco
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Note generali: Description based upon print version of record.
• Nota di bibliografia: Includes bibliographical references at the end of each chapters and index.
• Nota di contenuto: Protein Phosphorylation; Preface; Contents; List of contributors; List of Abbreviations; 1 The brain of the cell; 1.1 Signals and symbols; 1.2 Proteins as communicative molecules; 1.3 The discovery of protein phosphorylation; 1.4 Protein phosphorylation in prokaryotes; 1.5 Protein phosphorylation in eukaryotes; 1.5.1 Eukaryotic protein kinases: common features and diversities; 1.5.2 Control of protein kinase activity; 1.5.3 The problem of substrate specificity; 1.5.4 Regulatory signals for protein kinases and examples of signaling cross-talk; 1.5.5 Protein tyrosine phosphorylation and the integrity of multicellular organisms1.6 Signal extinction by protein dephosphorylation; 1.7 Cancer: a cellular 'psychosis'; 1.8 Advancing beyond the metaphor: proteins as non-trivial machines; References; 2 cAMP-dependent protein kinase: structure, function and control; 2.1 Introduction; 2.2 Biochemistry of cAPK; 2.2.1 Principles of purification of cAPK; 2.2.2 The ; catalytic subunit (C-subunit); 2.2.3 Control of cAPK; 2.3 Cellular aspects of cAPK function and control; 2.3.1 In vivo control of cAPK; 2.3.2 Cellular location of cAPK subunits; 2.4 Structural aspects of cAPK function2.4.1 Dynamics of substrate-induced fit in solution; 2.4.2 Crystal structure of cAPK C-subunit; 2.4.3 Aspects of future research on cAPK; 2.5 A quick look at the cGMP-dependent protein kinase: a close relative of cAPK; 2.6 Structural consequences of protein phosphorylation in general; 2.6.1 Immediate physical consequences; 2.6.2 Conformational change - indirect evidence; 2.6.3 Conformational change - direct evidence; 2.6.4 Structural effects in peptides; References; 3 Protein kinase C; 3.1 Introduction; 3.2 The protein kinase C isoenzyme family; 3.2.1 The PKC subfamilies3.2.2 PKC isoenzyme structures: common features and differences3; 3.2.3 Regulation of PKC activity4; 3.3 Cellular functions of protein kinase C; 3.3.1 Activators and inhibitors as tools in PKC research; 3.3.2 Phorbol ester effects; 3.3.3 Are effects of phorbol esters and DAG reliable indicators of PKC action?; 3.3.4 Effects of altered PKC expression on cellular functions; 3.3.5 PKC substrates11; 3.3.6 How PKC may acquire substrate specificity; 3.4 Protein kinase C in disease; 3.4.1 Involvement of PKC expression in benign and malignant hyperproliferative diseases; 3.4.2 Oncogenic and anti-oncogenic effects of protein kinase C expression3.4.3 Protein kinase C and skin tumor promotion; References; 4 Casein kinases; 4.1 The different classes of casein kinases; 4.2 Protein kinase CK2; 4.2.1 History; 4.2.2 Biochemical features; 4.2.3 Molecular structures. interaction of subunits and regulation mechanisms; 4.2.4 CK2 genes and their chromosomal locations; 4.2.5 Transcribed CK2 messages and transcription control; 4.2.6 Cell physiological roles of CK2; 4.2.7 CK2 in mitogenic signal transmission; 4.2.8 CK2 and the cell cycle; 4.3 Protein kinase CK1; 4.3.1 Biochemical features and molecular structures of CK1
• Sommario/riassunto: Protein phosphorylation is a key mechanism in cellular signaling. This volume presents a state-of-the-art survey of one of the most rapidly developing fields of biochemical research. Written by leading experts, it presents the latest results for some of the most important cellular pathways. Color plates illustrate structural or functional relationships, numerous references provide links to the original literature.