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This book provides the most updated information of how membrane lipids mediate protein signaling from studies carried out in animal and plant cells. Also, there are some chapters that go beyond and expand these studies of protein-lipid interactions at the structural level. The book begins with a literature review from investigations associated to sphingolipids, followed by studies that describe the role of phosphoinositides in signaling and closing with the function of other key lipids in signaling at the plasma membrane and intracellular organelles.
Lipids traditionally have been viewed as serving two functions: to form cellular membranes and to serve as energy stores. During the last two decades, a new role for lipids has taken center stage: lipids can act as signalling molecules. This book deals with a variety of lipids that have been shown to be messengers. Leading scientists explore all known lipid classes except steroid hormones. Researchers and educators in biochemistry as well as in molecular and cellular biology will appreciate this volume.
This is the first compilation of protein lipidation enzymes. This volume summarizes recent dramatic developments regarding enzymes responsible for protein lipidation, a process critical for a number of physiological functions, including cell proliferation and morphology. Inhibitors of protein lipidation have recently been shown to be useful as anticancer drugs. Enzymatic mechanisms, mutational analysis, and structural studies are presented. The enzymatic mechanisms of protein lipidation Three-dimensional structures of protein farnesytransferase, protein geranylgeranytransferase II, and n-myristoryltransferase
Concise chapters, written by experts in the field, cover a wide spectrum of topics on lipid and membrane formation in microbes (Archaea, Bacteria, eukaryotic microbes).All cells are delimited by a lipid membrane, which provides a crucial boundary in any known form of life. Readers will discover significant chapters on microbial lipid-carrying biomolecules and lipid/membrane-associated structures and processes.
Lipidation is a post-translational modification that covalently attaches lipid groups to proteins to restrict their motility to the cell membrane. In this study, we proposed to induce artificial protein-membrane anchorage through the use of a rationally designed Protein-Membrane Anchor (PMA) to inhibit a protein's motility and function within the cell. We hypothesized that induced membrane anchorage of proteins can hold significant therapeutic value when applied to cancer-promoting cell-signaling proteins. Our proof-of-concept PMA 1 was able to sequester and immobilize STAT3, a 93 kDa protein, to the plasma membrane in breast cancer cells. To the best of our knowledge we are the first to design a PMA that targets and restricts the motility of a soluble cytosolic protein. Unfortunately, our second generation PMAs, which incorporated more drug-like, nonphosphorylated molecules, were unable to localize STAT3 to the plasma membrane. However, the PMAs did inhibit STAT3 nuclear translocation in IL6 stimulated breast cancer cells, suggesting that they might be anchoring STAT3 on intracellular membranes. To prevent the physiological drawbacks associated with using large lipidic groups on drugs, we designed prodrug-like PMAs that activate in situ, called PPB-PMAs. The PPB-PMAs incorporate a motif that is recognized by farnesyltransferase to install a farnesyl group, inducing membrane anchorage. Our proof-of-principle PPB was able to undergo farnesylation in an in vitro enzymatic assay as well as anchor in the plasma membrane in breast cancer cells. Currently, the PPB-PMA is being tested for its ability to anchor its target protein, FKBP12. The versatility of the PMA strategy was also demonstrated through the use of metal coordination complex PMAs. These PMAs were able to selectively immobilize phospho-peptides to lipid bilayers. The progress towards designing, synthesizing and testing the novel PMAs is reported herein.
A NATO Advanced Study Institute on "New Developments in Lipid-Protein Interactions and Receptor Function" was held on the Island of Spetsai, Greece, from August 16-27, 1992. This Institute was organized to bring together researchers in the field of membrane organization and dynamics with those actively involved in studies on receptor function, signal transduction mechanisms and gene regulation. 2 Presentations and discussions focussed on the regulation of intracellular Ca +-levels, on the second messengers derived from inositol lipids and on the specific phospholipase C isozymes involved in these processes. A major focus was on G-proteins and the effect of lipid anchors on their function. These principles of regulation were further discussed in the context of receptors for acetylcholine, lysophosphatidic acid and low-density lipoproteins. In addition, various aspects of the genomic regulation of cell growth and differentiation by transcription factors were presented. These topics were put into perspective by discussing the most recent developments in lipid-protein interactions, protein insertion into membranes, membrane lipid organization and lipid dynamics as mediated by phospholipid transfer proteins. This book presents the content of the major lectures and a selection of the most relevant of the most important topics posters. These proceedings offer a comprehensive account presented during the course of the Institute. The book is intended to make these proceedings accessible to a large audience.
It is well established that cellular lipid binding proteins serve central roles in cellular lipid uptake and metabolism. Evidence has been presented that various metabolic diseases, such as hyperlipidemia, atherosclerosis, insulin resistance, and diabetes, are characterized by malfunctioning or deficiencies in cellular lipid binding proteins. For better understanding of the action of lipids as signaling compounds and the role of lipids in intermediary metabolism, it is essential to have detailed knowledge of the interactions between lipids and their cognant binding proteins. In view of this growing interest in lipid-protein interaction, the 4th International Conference on Lipid Binding Proteins was held in Maastricht, The Netherlands, in June 2001. The proceedings of the previous three meetings have been published in Molecular and Cellular Biochemistry. The present focused issue of Molecular and Cellular Biochemistry comprises selected papers based on the lectures and posters presented during the 4th conference, and provides insight into the significance of these proteins for the functioning of the cell.
As the highly anticipated update to Lipid Second Messengers (CRC Press, 1999), Lipid-Mediating Signaling is a current and comprehensive overview of research methods used in lipid-mediated signal transduction. Pioneering experts provide a much-needed distillation of a decade's worth of advances in research techniques that are pertinent in understand
Lipidation is a post-translational modification that covalently attaches lipid groups to proteins to restrict their motility to the cell membrane. In this study, we proposed to induce artificial protein-membrane anchorage through the use of a rationally designed Protein-Membrane Anchor (PMA) to inhibit a protein's motility and function within the cell. We hypothesized that induced membrane anchorage of proteins can hold significant therapeutic value when applied to cancer-promoting cell-signaling proteins. Our proof-of-concept PMA 1 was able to sequester and immobilize STAT3, a 93 kDa protein, to the plasma membrane in breast cancer cells. To the best of our knowledge we are the first to design a PMA that targets and restricts the motility of a soluble cytosolic protein. Unfortunately, our second generation PMAs, which incorporated more drug-like, nonphosphorylated molecules, were unable to localize STAT3 to the plasma membrane. However, the PMAs did inhibit STAT3 nuclear translocation in IL6 stimulated breast cancer cells, suggesting that they might be anchoring STAT3 on intracellular membranes. To prevent the physiological drawbacks associated with using large lipidic groups on drugs, we designed prodrug-like PMAs that activate in situ, called PPB-PMAs. The PPB-PMAs incorporate a motif that is recognized by farnesyltransferase to install a farnesyl group, inducing membrane anchorage. Our proof-of-principle PPB was able to undergo farnesylation in an in vitro enzymatic assay as well as anchor in the plasma membrane in breast cancer cells. Currently, the PPB-PMA is being tested for its ability to anchor its target protein, FKBP12. The versatility of the PMA strategy was also demonstrated through the use of metal coordination complex PMAs. These PMAs were able to selectively immobilize phospho-peptides to lipid bilayers. The progress towards designing, synthesizing and testing the novel PMAs is reported herein.