Regulation and Function of Protein Kinases and Phosphatases
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Enzyme Research Regulation and Function of Protein Kinases and Phosphatases Guest Editors: Heung-Chin Cheng, Robert Z. Qi, Hemant Paudel, and Hong-Jian Zhu Regulation and Function of Protein Kinases and Phosphatases Enzyme Research Regulation and Function of Protein Kinases and Phosphatases Guest Editors: Heung-Chin Cheng, Robert Z. Qi, Hemant Paudel, and Hong-Jian Zhu Copyright © 2011 SAGE-Hindawi Access to Research. All rights reserved. This is a special issue published in volume 2011 of “Enzyme Research.” All articles are open access articles distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Editorial Board Sabbir Ahmed, UK D. M. G. Freire, Brazil Michael J. McLeish, USA Mario Amzel, USA Vilmos Fulop, UK William David Nes, USA Vasu D. Appanna, Canada Giovanni Gadda, USA Toshihisa Ohshima, Japan David Ballou, USA J. Guisan, Spain Michael Page, UK Ulrich Baumann, Switzerland Munishwar Nath Gupta, India Jose Miguel Palomo, Spain Fabrizio Briganti, Italy R. S. Gupta, Canada Robert Pike, Australia Joaquim Cabral, Portugal Albert Jeltsch, Germany Raffaele Porta, Italy Gerald M. Carlson, USA Marilyn S. Jorns, USA Alireza R. Rezaie, USA Sunney I. Chan, USA Mari Kaartinen, Canada Ali-Akbar Saboury, Iran Christopher Davies, USA Eva N. Karlsson, Sweden Engin Serpersu, USA Narasimha R. Desirazu, India Leszek Kleczkowski, Sweden Assia Shisheva, USA John David Dignam, USA William Konigsberg, USA R. D. Tanner, USA Colin Dingwall, UK H. Kuhn, Germany John J. Tanner, USA Jean-Marie Dupret, France David Lambeth, USA Gianluigi Veglia, USA Paul Engel, Ireland A-Lien Lu-Chang, USA Qi-Zhuang Ye, USA Roberto F. Lafuente, Spain Paul Malthouse, Ireland Contents Regulation and Function of Protein Kinases and Phosphatases, Heung-Chin Cheng, Robert Z. Qi, Hemant Paudel, and Hong-Jian Zhu Volume 2011, Article ID 794089, 3 pages Asp295 Stabilizes the Active-Site Loop Structure of Pyruvate Dehydrogenase, Facilitating Phosphorylation of Ser292 by Pyruvate Dehydrogenase-Kinase, Tripty A. Hirani, Alejandro Tovar-Mendez,´ Jan´ A. Miernyk, and Douglas D. Randall Volume 2011, Article ID 939068, 13 pages Relative Expression Levels Rather Than Specific Activity Plays the Major Role in Determining In Vivo AKT Isoform Substrate Specificity, Rachel S. Lee, Colin M. House, Briony E. Cristiano, Ross D. Hannan, Richard B. Pearson, and Katherine M. Hannan Volume 2011, Article ID 720985, 18 pages Determinants for Substrate Specificity of Protein Phosphatase 2A, Andrew M. Slupe, Ronald A. Merrill, and Stefan Strack Volume 2011, Article ID 398751, 8 pages Control of Genetically Prescribed Protein Tyrosine Kinase Activities by Environment-Linked Redox Reactions, Izumi Nakashima, Yoshiyuki Kawamoto, Kozue Takeda, and Masashi Kato Volume 2011, Article ID 896567, 10 pages Inorganic Phosphate as an Important Regulator of Phosphatases, Claudia Fernanda Dick, AndreLuizAra´ ujo´ Dos-Santos, and JoseRobertoMeyer-Fernandes´ Volume 2011, Article ID 103980, 7 pages Interaction between Calcineurin and Ca2+/Calmodulin Kinase-II in Modulating Cellular Functions, Manabu Kubokawa, Kazuyoshi Nakamura, and You Komagiri Volume 2011, Article ID 587359, 5 pages Canonical and Alternative Pathways in Cyclin-Dependent Kinase 1/Cyclin B Inactivation upon M-Phase Exit in Xenopus laevis Cell-Free Extracts, Jacek Z. Kubiak and Mohammed El Dika Volume 2011, Article ID 523420, 8 pages Protein Kinase C and Toll-Like Receptor Signaling, Daniel J. Loegering and Michelle R. Lennartz Volume 2011, Article ID 537821, 7 pages Protein Kinases and Phosphatases in the Control of Cell Fate, Angela Bononi, Chiara Agnoletto, Elena De Marchi, Saverio Marchi, Simone Patergnani, Massimo Bonora, Carlotta Giorgi, Sonia Missiroli, Federica Poletti, Alessandro Rimessi, and Paolo Pinton Volume 2011, Article ID 329098, 26 pages Acid Phosphatases of Budding Yeast as a Model of Choice for Transcription Regulation Research, Elena V. Sambuk, Anastasia Yu. Fizikova, Vladimir A. Savinov, and Marina V. Padkina Volume 2011, Article ID 356093, 16 pages Phosphorylcholine Phosphatase: A Peculiar Enzyme of Pseudomonas aeruginosa, Carlos Eduardo Domenech, Lisandro Horacio Otero, Paola Rita Beassoni, and Angela Teresita Lisa Volume 2011, Article ID 561841, 12 pages SAGE-Hindawi Access to Research Enzyme Research Volume 2011, Article ID 794089, 3 pages doi:10.4061/2011/794089 Editorial Regulation and Function of Protein Kinases and Phosphatases Heung-Chin Cheng,1 Robert Z. Qi,2 Hemant Paudel,3, 4 and Hong-Jian Zhu5 1 Department of Biochemistry & Molecular Biology, Bio21 Molecular Sciences and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3010, Australia 2 Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China 3 Bloomfield Center for Research in Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis-Jewish General Hospital, Montreal, QC, Canada H3T 1E2 4 The Department of Neurology and Neurosurgery, McGill University, Montreal, QC, Canada H3T 1E2 5 Department of Surgery, Royal Melbourne Hospital, The University of Melbourne, Parkville, VIC 3052, Australia Correspondence should be addressed to Heung-Chin Cheng, [email protected] Received 3 November 2011; Accepted 3 November 2011 Copyright © 2011 Heung-Chin Cheng et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Protein kinases and phosphatases are enzymes catalysing the changes induced by phosphorylation are highly dependent transfer of phosphate between their substrates. A protein on the structural context of the phosphorylated protein. kinase catalyses the transfer of γ-phosphate from ATP (or Upon phosphorylation, the phosphate group regulates the GTP) to its protein substrates while a protein phosphatase activity of the protein by creating a network of hydrogen catalyses the transfer of the phosphate from a phospho- bonds among specific amino acid residues nearby. This protein to a water molecule. Even though both groups of network of hydrogen bonds is governed by the three- enzymes are phosphotransferases, they catalyse opposing dimensional structure of the phosphorylated protein and reactions to modulate the structures and functions of many therefore is unique to each protein. The most notable exam- cellular proteins in prokaryotic and eukaryotic cells. Among ple of regulation of protein function by phosphorylation- the various types of posttranslational modifications, protein induced conformational changes is glycogen phosphorylase phosphorylation and dephosphorylation are the most preva- [4]. Glycogen phosphorylase, made up of two identical lent modifications regulating the structures and functions of subunits, is activated upon phosphorylation of Ser-14 of cellular proteins in a wide spectrum of cellular processes, each subunit by phosphorylase kinase [4]. Phosphorylation ranging from cell fate control to regulation of metabolism. of Ser-14 in one monomer creates a network of hydrogen For example, even though protein kinase genes constitute bonds between the phosphate group and the side chains of only 2% of the genomes in most eukaryotes, protein kinases Arg-43 of the same monomer as well as Arg-69 of the other phosphorylate more than 30% of the cellular proteins monomeric subunit [5]. This network induces significant [1]. Owing to the significant roles of protein kinases and intra- and intersubunit configurational changes, allowing phosphatases in cellular regulation, this special issue focuses access of the substrates to the active sites and appropriately on their regulation, and functions. In this issue, there are two aligning the catalytically critical residues in the active sites research articles and seven reviews on various topics related for catalysis of the phosphorolysis reaction. to the structure, regulation and functions of protein kinases Phosphorylation can also modulate the function of a and phosphatases. Together, they give the readers a glimpse protein by disrupting the surfaces for protein-ligand in- of the roles played by protein kinases and phosphatases in teractions without inducing any conformational changes. regulating many physiological processes in both prokaryotic For example, phosphorylation of Ser-113 of the bacterial and eukaryotic cells. They also highlight the complexity of isocitrate dehydrogenase almost completely inactivates the the regulation of protein kinases and phosphatases. enzyme without inducing any significant conformational Phosphorylation regulates protein functions by inducing changes [6, 7]. The phosphate group attached to Ser-113 conformational changes or by disruption and creation of simply blocks binding of the enzyme to isocitrate. Like- protein-protein interaction surfaces [2, 3]. Conformational wise, phosphorylation can also create ligand-binding surface 2 Enzyme Research without inducing conformational changes. For example, Substrate specificity of protein phosphatases is governed tyrosine phosphorylation of some cellular proteins creates by interactions between interaction motifs or domains the binding sites for SH2 domains and PTB domains [8, 9]. located distally from the phosphatase active site and distal The functions of protein kinases and phosphatases are docking motifs spatially separated from the target phos- mediated by