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Biology of Phosphoinositides
Edited by Shamshad Cockcroft
366 pages
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numerous figures
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246x189mm
978-0-19-963764-5
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Paperback
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20 April 2000
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This item is printed to order and supplied on a firm sale basis. Items which are printed to order are normally despatched and charged within 5-10 days.
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- Well illustrated with over 75 figures.
Phosphoinostides have been known to play a role in cell signalling since the 1950s and since then, lipid signals have been discovered to play a role in many different cellular functions. Biology of Phosphoinostides is not a historical account, but a review of the current opinions of lipid signalling research with the emphasis on the integration of the use of lipid signals in signal transduction and membrane trafficking. These two areas have traditionally been seen as separate but now anyone ignoring one area at the expense of the other does so at their peril. The regulation of phospholipase C (and its
isozymes), phospholipase D, the phosphinositide-3-kinases, chloride channel conductance by inositol (3,4,5,6) tetraphosphate, and of cytoskeletal protein activity by inositol lipids are all covered in depth. There is specific discussion of the PH and FYVE lipid binding domains that allow lipids to control the movement, location, and activation- state of membrane proteins. The central issue of the control of synthesis, translocation, and degradation of phosphoinositides is also given due coverage. For too long, lipids have been seen as a backwater of biology and an uninteresting topic to study. However their central role in cell function is now properly recognized and the Biology of Phosphoinositides will serve as an enjoyable and intriguing introduction to what these slippery molecules
can achieve.Readership: Postgraduate researchers and lecturers working on signal transduction or membrane trafficking. Anyone interested in the role of lipids in cellular function.
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Edited by Shamshad Cockcroft, Department of Physiology, University College London Contributors:
Vytas A. Bankaitis, Dept. of Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294-0005 USA; Mark A. Carew, Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA; Christopher Carpenter, Beth Israel Deaconess Medical Centre, Harvard Institutes of Medicine, 330 Brookline Avenue, Boston, MA 02215, USA; Kathryn M. Ferguson, Department of Biochemistry and Biophysics, University of Pennsylvania, School of Medicine, Philadelphia, A606 Richards Building, 3700
Hamilton Walk, Philadelphia PA 19104-6089, USA; Lisa A. Flanagan, Haematology Division, LMRC 312, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, MA 02445, USA; Michael A. Frohman, Department of Pharmacology, SUNY-Stony Brook, Stony Brook NY 11794, USA; Philip Hawkins, Inositide Laboratory, Babraham Institute, Babraham Cambridge CB2 4AT; Mellisa W. Y. Ho, Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709 USA; Paul A. Janmey, Haematology Division, LMRC 312, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, MA 02445, USA; Sang Bong Lee, Laboratory of Cell Signalling, National Heart, Lung and Blood Institute, National Institute of Health, Bethesda, Maryland 20892-0320, USA; Mark Lemmon, Department of
Biochemistry and Biophysics, University of Pennsylvania, School of Medicine, Philadelphia, A606 Richards Buildings, 3700 Hamilton Walk, Philadelphia PA 19104-6089, USA; Xinmin Li, Department of Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294-0005, USA; Martin G. Low, Dept. of Physiology & Cellular Biophysics, Columbia University Health Sciences, W. 168th Street, New York, NY 10032, USA; Alex McGregor, Inositide Laboratory, Babraham Institute, Babraham Cambridge, CB2 4AT; Andrew J. Morris, Department of Pharmacology, SUNY-Stony Brook, Stony Brook, NY 11794, USA; Peter Parker, Protein Phosphorylation Group, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX; Benoit Poulin, Laboratory of Cell Signalling, National Heart Lung and Blood
Institute, National Institute of Health, Bethesda, Maryland 20892-0320, USA; Sue Goo Rhee, Laboratory of Cell Signalling, National Heart Lung and Blood Institute, National Institute of Health, Bethesda, Maryland 20892-0320, USA; Marcos P. Rivas, Department of Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294-0005, USA; Vicki A. Sciorra, Department of Pharmacology, SUNY-Stony Brook, Stony Brook, NY 11794, USA; Fujio Sekiya, Laboratory of Cell Signalling, National Heart Lung and Blood Institute, National Institute of Health, Bethesda, Maryland 20892-0320, USA; Stephen Shears, Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA; Harald Stenmark, Dept. of Biochemistry, The Norwegian Radium
Hospital, Montebello, N-0310 Oslo, Norway; Len Stephens, Inositide Laboratory, Babraham Institute, Babraham Cambridge CB2 4AT; Kimberley Tolias, Beth Israel Deaconess Medical Centre, Harvard Institutes of Medicine, 330 Brookline Avenue, Boston MA 02215, USA; Rudiger Woscholski, Protein Phosphorylation Group, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX; Xiaonian Yang, Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA
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Regulation of Phosphoinositide-specific Phospholipase C isozymes
Phosphoinositide- 3-kinases - Regulation by cell surface receptors and function of 3-phosphorylated lipids
Enzymes involved in the synthesis of phosphatidylinositol 4,5 bisphosphate and their regulation - Phosphoinositide kinases
Pleckstrin Homology Domains: Phosphoinositide-regulated membrane tethers
Regulation of cytoskeletal protein by inositol lipids
Physiological functions phosphatidylinositol transfer proteins
Glycosyl-phosphatidylinositol anchored proteins and their phospholipases
Phosphatidylinositol 3 kinase and membrane traffic
Regulation of Phospholipase D signalling by phosphoinositides
Regulation of chloride channel conductance by inositol (3,4,5,6) tetraphosphate; A phosphoinositide-initiated signalling pathway that acts downstream of inositol (1,4,5) trisphosphate
Phosphatases for inositol lipids and for inositol phosphates
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