John David York
Adjunct Professor in the Department of Pharmacology & Cancer Biology
My laboratory is interested in the biology of cellular
communication networks and the mechanisms by which defects in these
pathways contribute to the pathophysiology of human disease. We
study a widely utilized communication network, the inositol signal
transduction pathway. The classic paradigm of inositol signaling
activation is that receptor stimulation leads to the breakdown of an
inositol lipid precursor into two second messengers inositol
1,4,5-trisphosphate (IP3) and 1,2-diacylglycerol, which regulate
calcium release and protein kinase C, respectively. However, in
recent years the tremendous complexity of the inositol metabolic
pathway has become evident. Diverse stimuli from growth factors to
light activate molecular programs that lead to the production of
numerous inositol polyphosphate (IP) messenger molecules. In all,
over 30 lipid and water-soluble IP molecules have been identified in
eukaryotic cells, many of which have not yet been assigned a function
in cells and hence have been designated as "orphan" IP molecules.
Our research efforts have focused on expanding the understanding of
the pathway by seeking to identify the cellular targets and processes
influenced by "orphan" IP messengers. We have utilized a
multidisciplinary approach, which includes Pharmacology,
Biochemistry, Genetics, Biophysics and Cell Molecular Biology, to
characterize the function of over ten gene products that regulate the
synthesis and breakdown of these molecules. Our work has helped
identify new roles for "orphan" IP messengers in the regulation of
diverse processes including membrane trafficking, cytoskeletal
organization, gene expression, and mRNA export. Furthermore, we have
found that an additional layer of complexity is achieved through the
compartmentalization of IP pathways to the nucleus. In addition, by
determining the X-ray crystal structure of one of the enzymes we have
uncovered a novel family of lithium targets with relevance to manic
depressive disease. These discoveries have led us to revise the
classic paradigm of inositol signaling to include several new
inositol second messengers and have uncovered new areas of research
aimed at understanding a fundamental problem in biology - that of how
diverse stimuli utilize IP signaling pathways to achieve specific
cellular responses.
communication networks and the mechanisms by which defects in these
pathways contribute to the pathophysiology of human disease. We
study a widely utilized communication network, the inositol signal
transduction pathway. The classic paradigm of inositol signaling
activation is that receptor stimulation leads to the breakdown of an
inositol lipid precursor into two second messengers inositol
1,4,5-trisphosphate (IP3) and 1,2-diacylglycerol, which regulate
calcium release and protein kinase C, respectively. However, in
recent years the tremendous complexity of the inositol metabolic
pathway has become evident. Diverse stimuli from growth factors to
light activate molecular programs that lead to the production of
numerous inositol polyphosphate (IP) messenger molecules. In all,
over 30 lipid and water-soluble IP molecules have been identified in
eukaryotic cells, many of which have not yet been assigned a function
in cells and hence have been designated as "orphan" IP molecules.
Our research efforts have focused on expanding the understanding of
the pathway by seeking to identify the cellular targets and processes
influenced by "orphan" IP messengers. We have utilized a
multidisciplinary approach, which includes Pharmacology,
Biochemistry, Genetics, Biophysics and Cell Molecular Biology, to
characterize the function of over ten gene products that regulate the
synthesis and breakdown of these molecules. Our work has helped
identify new roles for "orphan" IP messengers in the regulation of
diverse processes including membrane trafficking, cytoskeletal
organization, gene expression, and mRNA export. Furthermore, we have
found that an additional layer of complexity is achieved through the
compartmentalization of IP pathways to the nucleus. In addition, by
determining the X-ray crystal structure of one of the enzymes we have
uncovered a novel family of lithium targets with relevance to manic
depressive disease. These discoveries have led us to revise the
classic paradigm of inositol signaling to include several new
inositol second messengers and have uncovered new areas of research
aimed at understanding a fundamental problem in biology - that of how
diverse stimuli utilize IP signaling pathways to achieve specific
cellular responses.
Current Appointments & Affiliations
- Adjunct Professor in the Department of Pharmacology & Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 2012
Contact Information
- C203 Lev Sci Res Ctr, Durham, NC 27708
- Duke Box 3813, Durham, NC 27710
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yorkj@duke.edu
(919) 681-6414
- Background
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Education, Training, & Certifications
- Postdoctoral Fellow, Washington University in St. Louis 1993 - 1994
- Teaching Assistant, Washington University in St. Louis 1992 - 1993
- Ph.D., Washington University in St. Louis 1993
- Research Assistant, Washington University in St. Louis 1990 - 1992
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Previous Appointments & Affiliations
- Cancer Biology Professor of Pharmacology and Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 2009 - 2020
- Professor of Biochemistry, Biochemistry, Basic Science Departments 2008 - 2019
- Member of the Duke Cancer Institute, Duke Cancer Institute, Institutes and Centers 1996 - 2014
- Professor of Pharmacology & Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 2008 - 2012
- Associate Professor of Biochemistry, Biochemistry, Basic Science Departments 2002 - 2008
- Associate Professor of Pharmacology & Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 2002 - 2008
- Assistant Professor of Pharmacology & Cancer Biology, Pharmacology & Cancer Biology, Basic Science Departments 1996 - 2002
- Assistant Professor of Biochemistry, Biochemistry, Basic Science Departments 1997 - 2002
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Academic Positions Outside Duke
- Research Instructor, Washington University in St. Louis. 1994 - 1996
- Recognition
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Awards & Honors
- Research
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Selected Grants
- The Biology of Inositol Polyphosphate Signaling awarded by National Institutes of Health 1996 - 2012
- Analysis of PH1-Associated Alanine:Glyoxylate Aminotranferase (AGT) Using Yeast awarded by National Institutes of Health 2008 - 2011
- Replacement Equipment Components for an 800 MHz NMR Spectrometer awarded by National Institutes of Health 2010 - 2011
- Identification of pharmacological chaperones for misfolded proteins awarded by National Institutes of Health 2008 - 2011
- Developing inhibitors of RalA function for the treatment of pancreatic cancer awarded by National Institutes of Health 2007 - 2009
- Biological Oscilloscopes: Spatio-Temporal Metabolomics awarded by National Institutes of Health 2004 - 2008
- Publications & Artistic Works
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Selected Publications
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Academic Articles
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Bersell, Kevin R., Tao Yang, Jonathan D. Mosley, Andrew M. Glazer, Andrew T. Hale, Dmytro O. Kryshtal, Kyungsoo Kim, et al. “Transcriptional Dysregulation Underlies Both Monogenic Arrhythmia Syndrome and Common Modifiers of Cardiac Repolarization.” Circulation 147, no. 10 (March 7, 2023): 824–40. https://doi.org/10.1161/CIRCULATIONAHA.122.062193.Full Text Link to Item
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Xu, Pengfei, Yue Xi, Pengcheng Wang, Zigmund Luka, Meishu Xu, Hung-Chun Tung, Jingyuan Wang, et al. “Inhibition of p53 Sulfoconjugation Prevents Oxidative Hepatotoxicity and Acute Liver Failure.” Gastroenterology 162, no. 4 (April 2022): 1226–41. https://doi.org/10.1053/j.gastro.2021.12.260.Full Text Link to Item
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Eisele, Brynna S., Alice J. Wu, Zigmund Luka, Andrew T. Hale, and John D. York. “Bisphosphate nucleotidase 2 (BPNT2), a molecular target of lithium, regulates chondroitin sulfation patterns in the cerebral cortex and hippocampus.” Advances in Biological Regulation 83 (January 2022): 100858. https://doi.org/10.1016/j.jbior.2021.100858.Full Text
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Eisele, Brynna S., Zigmund Luka, Alice J. Wu, Fei Yang, Andrew T. Hale, and John D. York. “Sulfation of glycosaminoglycans depends on the catalytic activity of lithium-inhibited phosphatase BPNT2 in vitro.” J Biol Chem 297, no. 5 (November 2021): 101293. https://doi.org/10.1016/j.jbc.2021.101293.Full Text Link to Item
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Xu, Pengfei, Yue Xi, Junjie Zhu, Min Zhang, Zigmund Luka, Donna B. Stolz, Xinran Cai, et al. “Intestinal Sulfation Is Essential to Protect Against Colitis and Colonic Carcinogenesis.” Gastroenterology 161, no. 1 (July 2021): 271-286.e11. https://doi.org/10.1053/j.gastro.2021.03.048.Full Text Link to Item
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Dollins, D Eric, Jian-Ping Xiong, Stuart Endo-Streeter, David E. Anderson, Vinay S. Bansal, Jay W. Ponder, Yi Ren, and John D. York. “A structural basis for lithium and substrate binding of an inositide phosphatase.” J Biol Chem 296 (2021): 100059. https://doi.org/10.1074/jbc.RA120.014057.Full Text Link to Item
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Hale, Andrew T., Rachel E. Brown, Zigmund Luka, Benjamin H. Hudson, Pranathi Matta, Christopher S. Williams, and John D. York. “Modulation of sulfur assimilation metabolic toxicity overcomes anemia and hemochromatosis in mice.” Adv Biol Regul 76 (May 2020): 100694. https://doi.org/10.1016/j.jbior.2020.100694.Full Text Link to Item
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Dollins, D Eric, Wenli Bai, Peter C. Fridy, James C. Otto, Julie L. Neubauer, Samuel G. Gattis, Kavi P. M. Mehta, and John D. York. “Vip1 is a kinase and pyrophosphatase switch that regulates inositol diphosphate signaling.” Proc Natl Acad Sci U S A 117, no. 17 (April 28, 2020): 9356–64. https://doi.org/10.1073/pnas.1908875117.Full Text Link to Item
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Hale, Andrew T., Bradley P. Clarke, and John D. York. “Metabolic Labeling of Inositol Phosphates and Phosphatidylinositols in Yeast and Mammalian Cells.” Methods Mol Biol 2091 (2020): 83–92. https://doi.org/10.1007/978-1-0716-0167-9_7.Full Text Link to Item
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Clarke, Bradley P., Brandon L. Logeman, Andrew T. Hale, Zigmund Luka, and John D. York. “A synthetic biological approach to reconstitution of inositide signaling pathways in bacteria.” Adv Biol Regul 73 (August 2019): 100637. https://doi.org/10.1016/j.jbior.2019.100637.Full Text Link to Item
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McNamara, Dan E., Cole M. Dovey, Andrew T. Hale, Giovanni Quarato, Christy R. Grace, Cristina D. Guibao, Jonathan Diep, et al. “Direct Activation of Human MLKL by a Select Repertoire of Inositol Phosphate Metabolites.” Cell Chem Biol 26, no. 6 (June 20, 2019): 863-877.e7. https://doi.org/10.1016/j.chembiol.2019.03.010.Full Text Link to Item
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Dovey, Cole M., Jonathan Diep, Bradley P. Clarke, Andrew T. Hale, Dan E. McNamara, Hongyan Guo, Nathaniel W. Brown, et al. “MLKL Requires the Inositol Phosphate Code to Execute Necroptosis.” Mol Cell 70, no. 5 (June 7, 2018): 936-948.e7. https://doi.org/10.1016/j.molcel.2018.05.010.Full Text Link to Item
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Hudson, Benjamin H., Andrew T. Hale, Ryan P. Irving, Shenglan Li, and John D. York. “Modulation of intestinal sulfur assimilation metabolism regulates iron homeostasis.” Proc Natl Acad Sci U S A 115, no. 12 (March 20, 2018): 3000–3005. https://doi.org/10.1073/pnas.1715302115.Full Text Link to Item
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Hatch, Ace J., Audrey R. Odom, and John D. York. “Inositol phosphate multikinase dependent transcriptional control.” Adv Biol Regul 64 (May 2017): 9–19. https://doi.org/10.1016/j.jbior.2017.03.001.Full Text Link to Item
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Hargrove, Tatiana Y., Laura Friggeri, Zdzislaw Wawrzak, Aidong Qi, William J. Hoekstra, Robert J. Schotzinger, John D. York, F Peter Guengerich, and Galina I. Lepesheva. “Structural analyses of Candida albicans sterol 14α-demethylase complexed with azole drugs address the molecular basis of azole-mediated inhibition of fungal sterol biosynthesis.” J Biol Chem 292, no. 16 (April 21, 2017): 6728–43. https://doi.org/10.1074/jbc.M117.778308.Full Text Link to Item
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Seeds, Andrew M., Marco M. Tsui, Christine Sunu, Eric P. Spana, and John D. York. “Inositol phosphate kinase 2 is required for imaginal disc development in Drosophila.” Proc Natl Acad Sci U S A 112, no. 51 (December 22, 2015): 15660–65. https://doi.org/10.1073/pnas.1514684112.Full Text Link to Item
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Emptage, Ryan P., Nam K. Tonthat, John D. York, Maria A. Schumacher, and Pei Zhou. “Structural basis of lipid binding for the membrane-embedded tetraacyldisaccharide-1-phosphate 4'-kinase LpxK.” J Biol Chem 289, no. 35 (August 29, 2014): 24059–68. https://doi.org/10.1074/jbc.M114.589986.Full Text Link to Item
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Pulloor, Niyas Kudukkil, Sajith Nair, Kathleen McCaffrey, Aleksandar D. Kostic, Pradeep Bist, Jeremy D. Weaver, Andrew M. Riley, et al. “Human genome-wide RNAi screen identifies an essential role for inositol pyrophosphates in Type-I interferon response.” Plos Pathog 10, no. 2 (February 2014): e1003981. https://doi.org/10.1371/journal.ppat.1003981.Full Text Link to Item
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Hudson, Benjamin H., and John D. York. “Tissue-specific regulation of 3'-nucleotide hydrolysis and nucleolar architecture.” Adv Biol Regul 54 (January 2014): 208–13. https://doi.org/10.1016/j.jbior.2013.11.002.Full Text Link to Item
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Emptage, Ryan P., Charles W. Pemble, John D. York, Christian R. H. Raetz, and Pei Zhou. “Mechanistic characterization of the tetraacyldisaccharide-1-phosphate 4'-kinase LpxK involved in lipid A biosynthesis.” Biochemistry 52, no. 13 (April 2, 2013): 2280–90. https://doi.org/10.1021/bi400097z.Full Text Link to Item
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Hudson, Benjamin H., Joshua P. Frederick, Li Yin Drake, Louis C. Megosh, Ryan P. Irving, and John D. York. “Role for cytoplasmic nucleotide hydrolysis in hepatic function and protein synthesis.” Proc Natl Acad Sci U S A 110, no. 13 (March 26, 2013): 5040–45. https://doi.org/10.1073/pnas.1205001110.Full Text Link to Item
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Banfic, Hrvoje, Antonio Bedalov, John D. York, and Dora Visnjic. “Inositol pyrophosphates modulate S phase progression after pheromone-induced arrest in Saccharomyces cerevisiae.” J Biol Chem 288, no. 3 (January 18, 2013): 1717–25. https://doi.org/10.1074/jbc.M112.412288.Full Text Link to Item
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Endo-Streeter, Stuart, Man-Kin Marco Tsui, Audrey R. Odom, Jeremy Block, and John D. York. “Structural studies and protein engineering of inositol phosphate multikinase.” J Biol Chem 287, no. 42 (October 12, 2012): 35360–69. https://doi.org/10.1074/jbc.M112.365031.Full Text Link to Item
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Hudson, Benjamin H., and John D. York. “Roles for nucleotide phosphatases in sulfate assimilation and skeletal disease.” Adv Biol Regul 52, no. 1 (January 2012): 229–38. https://doi.org/10.1016/j.advenzreg.2011.11.002.Full Text Link to Item
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Hatch, Ace J., and John D. York. “SnapShot: Inositol phosphates.” Cell 143, no. 6 (December 10, 2010): 1030-1030.e1. https://doi.org/10.1016/j.cell.2010.11.045.Full Text Link to Item
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Monserrate, Jessica P., and John D. York. “Inositol phosphate synthesis and the nuclear processes they affect.” Curr Opin Cell Biol 22, no. 3 (June 2010): 365–73. https://doi.org/10.1016/j.ceb.2010.03.006.Full Text Link to Item
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Otto, James C., and John D. York. “Molecular manipulation and analysis of inositol phosphate and pyrophosphate levels in Mammalian cells.” Methods Mol Biol 645 (2010): 47–60. https://doi.org/10.1007/978-1-60327-175-2_3.Full Text Link to Item
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Tsui, Marco M., and John D. York. “Roles of inositol phosphates and inositol pyrophosphates in development, cell signaling and nuclear processes.” Adv Enzyme Regul 50, no. 1 (2010): 324–37. https://doi.org/10.1016/j.advenzreg.2009.12.002.Full Text Link to Item
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Padmanabhan, Usha, D Eric Dollins, Peter C. Fridy, John D. York, and C Peter Downes. “Characterization of a selective inhibitor of inositol hexakisphosphate kinases: use in defining biological roles and metabolic relationships of inositol pyrophosphates.” J Biol Chem 284, no. 16 (April 17, 2009): 10571–82. https://doi.org/10.1074/jbc.M900752200.Full Text Link to Item
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Majerus, Philip W., and John D. York. “Phosphoinositide phosphatases and disease.” J Lipid Res 50 Suppl, no. Suppl (April 2009): S249–54. https://doi.org/10.1194/jlr.R800072-JLR200.Full Text Link to Item
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Lin, Hongying, Peter C. Fridy, Anthony A. Ribeiro, Jae H. Choi, Deb K. Barma, Günter Vogel, J. R. Falck, Stephen B. Shears, John D. York, and Georg W. Mayr. “Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases.” J Biol Chem 284, no. 3 (January 16, 2009): 1863–72. https://doi.org/10.1074/jbc.M805686200.Full Text Link to Item
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Frederick, Joshua P., A Tsahai Tafari, Sheue-Mei Wu, Louis C. Megosh, Shean-Tai Chiou, Ryan P. Irving, and John D. York. “A role for a lithium-inhibited Golgi nucleotidase in skeletal development and sulfation.” Proc Natl Acad Sci U S A 105, no. 33 (August 19, 2008): 11605–12. https://doi.org/10.1073/pnas.0801182105.Full Text Link to Item
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York, John D., and Daniel J. Lew. “IP7 guards the CDK gate.” Nat Chem Biol 4, no. 1 (January 2008): 16–17. https://doi.org/10.1038/nchembio0108-16.Full Text Link to Item
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Fridy, Peter C., James C. Otto, D Eric Dollins, and John D. York. “Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases.” J Biol Chem 282, no. 42 (October 19, 2007): 30754–62. https://doi.org/10.1074/jbc.M704656200.Full Text Link to Item
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Otto, James C., Patrick Kelly, Shean-Tai Chiou, and John D. York. “Alterations in an inositol phosphate code through synergistic activation of a G protein and inositol phosphate kinases.” Proc Natl Acad Sci U S A 104, no. 40 (October 2, 2007): 15653–58. https://doi.org/10.1073/pnas.0705729104.Full Text Link to Item
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Lee, Young-Sam, Sashidhar Mulugu, John D. York, and Erin K. O’Shea. “Regulation of a cyclin-CDK-CDK inhibitor complex by inositol pyrophosphates.” Science 316, no. 5821 (April 6, 2007): 109–12. https://doi.org/10.1126/science.1139080.Full Text Link to Item
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Mulugu, Sashidhar, Wenli Bai, Peter C. Fridy, Robert J. Bastidas, James C. Otto, D Eric Dollins, Timothy A. Haystead, Anthony A. Ribeiro, and John D. York. “A conserved family of enzymes that phosphorylate inositol hexakisphosphate.” Science 316, no. 5821 (April 6, 2007): 106–9. https://doi.org/10.1126/science.1139099.Full Text Link to Item
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Seeds, Andrew M., Joshua P. Frederick, Marco M. K. Tsui, and John D. York. “Roles for inositol polyphosphate kinases in the regulation of nuclear processes and developmental biology.” Adv Enzyme Regul 47 (2007): 10–25. https://doi.org/10.1016/j.advenzreg.2006.12.019.Full Text Link to Item
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Seeds, Andrew M., and John D. York. “Inositol polyphosphate kinases: regulators of nuclear function.” Biochem Soc Symp, no. 74 (2007): 183–97. https://doi.org/10.1042/BSS0740183.Full Text Link to Item
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Otto, James C., Sashidhar Mulugu, Peter C. Fridy, Shean-Tai Chiou, Blaine N. Armbruster, Anthony A. Ribeiro, and John D. York. “Biochemical analysis of inositol phosphate kinases.” Methods Enzymol 434 (2007): 171–85. https://doi.org/10.1016/S0076-6879(07)34010-X.Full Text Link to Item
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DeKroon, Robert, Jennifer B. Robinette, Anita B. Hjelmeland, Emma Wiggins, Morven Blackwell, Mirta Mihovilovic, Makoto Fujii, et al. “APOE4-VLDL inhibits the HDL-activated phosphatidylinositol 3-kinase/Akt Pathway via the phosphoinositol phosphatase SHIP2.” Circ Res 99, no. 8 (October 13, 2006): 829–36. https://doi.org/10.1161/01.RES.0000245479.03190.9f.Full Text Link to Item
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Stevenson-Paulik, Jill, Shean-Tai Chiou, Josh P. Frederick, June dela Cruz, Andrew M. Seeds, James C. Otto, and John D. York. “Inositol phosphate metabolomics: merging genetic perturbation with modernized radiolabeling methods.” Methods 39, no. 2 (June 2006): 112–21. https://doi.org/10.1016/j.ymeth.2006.05.012.Full Text Link to Item
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York, John D. “Regulation of nuclear processes by inositol polyphosphates.” Biochim Biophys Acta 1761, no. 5–6 (2006): 552–59. https://doi.org/10.1016/j.bbalip.2006.04.014.Full Text Link to Item
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Stevenson-Paulik, Jill, Robert J. Bastidas, Shean-Tai Chiou, Roy A. Frye, and John D. York. “Generation of phytate-free seeds in Arabidopsis through disruption of inositol polyphosphate kinases.” Proc Natl Acad Sci U S A 102, no. 35 (August 30, 2005): 12612–17. https://doi.org/10.1073/pnas.0504172102.Full Text Link to Item
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Seeds, Andrew M., Robert J. Bastidas, and John D. York. “Molecular definition of a novel inositol polyphosphate metabolic pathway initiated by inositol 1,4,5-trisphosphate 3-kinase activity in Saccharomyces cerevisiae.” J Biol Chem 280, no. 30 (July 29, 2005): 27654–61. https://doi.org/10.1074/jbc.M505089200.Full Text Link to Item
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Frederick, Joshua P., Deidre Mattiske, Jessica A. Wofford, Louis C. Megosh, Li Yin Drake, Shean-Tai Chiou, Brigid L. M. Hogan, and John D. York. “An essential role for an inositol polyphosphate multikinase, Ipk2, in mouse embryogenesis and second messenger production.” Proc Natl Acad Sci U S A 102, no. 24 (June 14, 2005): 8454–59. https://doi.org/10.1073/pnas.0503706102.Full Text Link to Item
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Winter-Vann, Ann M., Rudi A. Baron, Waihay Wong, June dela Cruz, John D. York, David M. Gooden, Martin O. Bergo, Stephen G. Young, Eric J. Toone, and Patrick J. Casey. “A small-molecule inhibitor of isoprenylcysteine carboxyl methyltransferase with antitumor activity in cancer cells.” Proc Natl Acad Sci U S A 102, no. 12 (March 22, 2005): 4336–41. https://doi.org/10.1073/pnas.0408107102.Full Text Link to Item
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Spiegelberg, Bryan D., June Dela Cruz, Tzuo-Hann Law, and John D. York. “Alteration of lithium pharmacology through manipulation of phosphoadenosine phosphate metabolism.” J Biol Chem 280, no. 7 (February 18, 2005): 5400–5405. https://doi.org/10.1074/jbc.M407890200.Full Text Link to Item
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York, Sally J., Blaine N. Armbruster, Patricia Greenwell, Thomas D. Petes, and John D. York. “Inositol diphosphate signaling regulates telomere length.” J Biol Chem 280, no. 6 (February 11, 2005): 4264–69. https://doi.org/10.1074/jbc.M412070200.Full Text Link to Item
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Fujii, Makoto, and John D. York. “A role for rat inositol polyphosphate kinases rIPK2 and rIPK1 in inositol pentakisphosphate and inositol hexakisphosphate production in rat-1 cells.” J Biol Chem 280, no. 2 (January 14, 2005): 1156–64. https://doi.org/10.1074/jbc.M412006200.Full Text Link to Item
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York, John D., and Tony Hunter. “Signal transduction. Unexpected mediators of protein phosphorylation.” Science 306, no. 5704 (December 17, 2004): 2053–55. https://doi.org/10.1126/science.1107225.Full Text Link to Item
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Seeds, Andrew M., Joshua C. Sandquist, Eric P. Spana, and John D. York. “A molecular basis for inositol polyphosphate synthesis in Drosophila melanogaster.” J Biol Chem 279, no. 45 (November 5, 2004): 47222–32. https://doi.org/10.1074/jbc.M408295200.Full Text Link to Item
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Plattner, Rina, Brenda J. Irvin, Shuling Guo, Kevin Blackburn, Andrius Kazlauskas, Robert T. Abraham, John D. York, and Ann Marie Pendergast. “A new link between the c-Abl tyrosine kinase and phosphoinositide signalling through PLC-gamma1.” Nat Cell Biol 5, no. 4 (April 2003): 309–19. https://doi.org/10.1038/ncb949.Full Text Link to Item
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Stevenson-Paulik, Jill, Audrey R. Odom, and John D. York. “Molecular and biochemical characterization of two plant inositol polyphosphate 6-/3-/5-kinases.” J Biol Chem 277, no. 45 (November 8, 2002): 42711–18. https://doi.org/10.1074/jbc.M209112200.Full Text Link to Item
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Alb, James G., Scott E. Phillips, Kathleen Rostand, Xiaoxia Cui, Jef Pinxteren, Laura Cotlin, Timothy Manning, et al. “Genetic ablation of phosphatidylinositol transfer protein function in murine embryonic stem cells.” Mol Biol Cell 13, no. 3 (March 2002): 739–54. https://doi.org/10.1091/mbc.01-09-0457.Full Text Link to Item
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Kontos, Christopher D., Eugene H. Cha, John D. York, and Kevin G. Peters. “The endothelial receptor tyrosine kinase Tie1 activates phosphatidylinositol 3-kinase and Akt to inhibit apoptosis.” Mol Cell Biol 22, no. 6 (March 2002): 1704–13. https://doi.org/10.1128/MCB.22.6.1704-1713.2002.Full Text Link to Item
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Tsujishita, Y., S. Guo, L. E. Stolz, J. D. York, and J. H. Hurley. “Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-phosphatase.” Cell 105, no. 3 (May 4, 2001): 379–89. https://doi.org/10.1016/s0092-8674(01)00326-9.Full Text Link to Item
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York, J. D., S. Guo, A. R. Odom, B. D. Spiegelberg, and L. E. Stolz. “An expanded view of inositol signaling.” Adv Enzyme Regul 41 (2001): 57–71. https://doi.org/10.1016/s0065-2571(00)00025-x.Full Text Link to Item
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Botelho, R. J., M. Teruel, R. Dierckman, R. Anderson, A. Wells, J. D. York, T. Meyer, and S. Grinstein. “Localized biphasic changes in phosphatidylinositol-4,5-bisphosphate at sites of phagocytosis.” J Cell Biol 151, no. 7 (December 25, 2000): 1353–68. https://doi.org/10.1083/jcb.151.7.1353.Full Text Link to Item
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Ives, E. B., J. Nichols, S. R. Wente, and J. D. York. “Biochemical and functional characterization of inositol 1,3,4,5, 6-pentakisphosphate 2-kinases.” J Biol Chem 275, no. 47 (November 24, 2000): 36575–83. https://doi.org/10.1074/jbc.M007586200.Full Text Link to Item
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Aharonovitz, O., H. C. Zaun, T. Balla, J. D. York, J. Orlowski, and S. Grinstein. “Intracellular pH regulation by Na(+)/H(+) exchange requires phosphatidylinositol 4,5-bisphosphate.” J Cell Biol 150, no. 1 (July 10, 2000): 213–24. https://doi.org/10.1083/jcb.150.1.213.Full Text Link to Item
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Odom, A. R., A. Stahlberg, S. R. Wente, and J. D. York. “A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control.” Science 287, no. 5460 (March 17, 2000): 2026–29. https://doi.org/10.1126/science.287.5460.2026.Full Text Link to Item
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Raucher, D., T. Stauffer, W. Chen, K. Shen, S. Guo, J. D. York, M. P. Sheetz, and T. Meyer. “Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion.” Cell 100, no. 2 (January 21, 2000): 221–28. https://doi.org/10.1016/s0092-8674(00)81560-3.Full Text Link to Item
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Meyer, T., and J. D. York. “Calcium-myristoyl switches turn on new lights.” Nat Cell Biol 1, no. 4 (August 1999): E93–95. https://doi.org/10.1038/12090.Full Text Link to Item
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York, J. D., A. R. Odom, R. Murphy, E. B. Ives, and S. R. Wente. “A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export.” Science 285, no. 5424 (July 2, 1999): 96–100. https://doi.org/10.1126/science.285.5424.96.Full Text Link to Item
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Rivas, M. P., B. G. Kearns, Z. Xie, S. Guo, M. C. Sekar, K. Hosaka, S. Kagiwada, J. D. York, and V. A. Bankaitis. “Pleiotropic alterations in lipid metabolism in yeast sac1 mutants: relationship to "bypass Sec14p" and inositol auxotrophy.” Mol Biol Cell 10, no. 7 (July 1999): 2235–50. https://doi.org/10.1091/mbc.10.7.2235.Full Text Link to Item
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Guo, S., L. E. Stolz, S. M. Lemrow, and J. D. York. “SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases.” J Biol Chem 274, no. 19 (May 7, 1999): 12990–95. https://doi.org/10.1074/jbc.274.19.12990.Full Text Link to Item
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Spiegelberg, B. D., J. P. Xiong, J. J. Smith, R. F. Gu, and J. D. York. “Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate.” J Biol Chem 274, no. 19 (May 7, 1999): 13619–28. https://doi.org/10.1074/jbc.274.19.13619.Full Text Link to Item
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Basu, S. S., J. D. York, and C. R. Raetz. “A phosphotransferase that generates phosphatidylinositol 4-phosphate (PtdIns-4-P) from phosphatidylinositol and lipid A in Rhizobium leguminosarum. A membrane-bound enzyme linking lipid a and ptdins-4-p biosynthesis.” J Biol Chem 274, no. 16 (April 16, 1999): 11139–49. https://doi.org/10.1074/jbc.274.16.11139.Full Text Link to Item
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Improta-Brears, T., A. R. Whorton, F. Codazzi, J. D. York, T. Meyer, and D. P. McDonnell. “Estrogen-induced activation of mitogen-activated protein kinase requires mobilization of intracellular calcium.” Proc Natl Acad Sci U S A 96, no. 8 (April 13, 1999): 4686–91. https://doi.org/10.1073/pnas.96.8.4686.Full Text Link to Item
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Kontos, C. D., T. P. Stauffer, W. P. Yang, J. D. York, L. Huang, M. A. Blanar, T. Meyer, and K. G. Peters. “Tyrosine 1101 of Tie2 is the major site of association of p85 and is required for activation of phosphatidylinositol 3-kinase and Akt.” Mol Cell Biol 18, no. 7 (July 1998): 4131–40. https://doi.org/10.1128/MCB.18.7.4131.Full Text Link to Item
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Stolz, L. E., W. J. Kuo, J. Longchamps, M. K. Sekhon, and J. D. York. “INP51, a yeast inositol polyphosphate 5-phosphatase required for phosphatidylinositol 4,5-bisphosphate homeostasis and whose absence confers a cold-resistant phenotype.” J Biol Chem 273, no. 19 (May 8, 1998): 11852–61. https://doi.org/10.1074/jbc.273.19.11852.Full Text Link to Item
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Stolz, L. E., C. V. Huynh, J. Thorner, and J. D. York. “Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae.” Genetics 148, no. 4 (April 1998): 1715–29. https://doi.org/10.1093/genetics/148.4.1715.Full Text Link to Item
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York, J. D., J. P. Xiong, and B. Spiegelberg. “Nuclear inositol signaling: a structural and functional approach.” Adv Enzyme Regul 38 (1998): 365–74. https://doi.org/10.1016/s0065-2571(97)00018-6.Full Text Link to Item
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Malik, N., V. P. Poltoratsky, J. D. York, M. R. Lieber, and T. H. Carter. “Is dna dependent protein kinase, dna-pk, a dual function (phospholipid/protein) kinase?” Faseb Journal 10, no. 6 (December 1, 1996).
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Poltoratsky, V. P., X. Shi, J. D. York, M. R. Lieber, and T. H. Carter. “Human DNA-activated protein kinase (DNA-PK) is homologous to phosphatidylinositol kinases.” J Immunol 155, no. 10 (November 15, 1995): 4529–33.Link to Item
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York, J. D., J. W. Ponder, and P. W. Majerus. “Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure.” Proc Natl Acad Sci U S A 92, no. 11 (May 23, 1995): 5149–53. https://doi.org/10.1073/pnas.92.11.5149.Full Text Link to Item
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York, J. D., J. W. Ponder, Z. W. Chen, F. S. Mathews, and P. W. Majerus. “Crystal structure of inositol polyphosphate 1-phosphatase at 2.3-A resolution.” Biochemistry 33, no. 45 (November 15, 1994): 13164–71. https://doi.org/10.1021/bi00249a002.Full Text Link to Item
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York, J. D., J. E. Saffitz, and P. W. Majerus. “Inositol polyphosphate 1-phosphatase is present in the nucleus and inhibits DNA synthesis.” J Biol Chem 269, no. 31 (August 5, 1994): 19992–99.Link to Item
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York, J. D., and P. W. Majerus. “Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells.” J Biol Chem 269, no. 11 (March 18, 1994): 7847–50.Link to Item
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York, J. D., Z. W. Chen, J. W. Ponder, A. K. Chauhan, F. S. Mathews, and P. W. Majerus. “Crystallization and initial X-ray crystallographic characterization of recombinant bovine inositol polyphosphate 1-phosphatase produced in Spodoptera frugiperda cells.” J Mol Biol 236, no. 2 (February 18, 1994): 584–89. https://doi.org/10.1006/jmbi.1994.1167.Full Text Link to Item
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York, J. D., and P. W. Majerus. “Erratum: Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells (Journal of Biological Chemistry (1994) 269 (7847-7850)).” Journal of Biological Chemistry 269, no. 49 (January 1, 1994): 31322.
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York, J. D., R. A. Veile, H. Donis-Keller, and P. W. Majerus. “Cloning, heterologous expression, and chromosomal localization of human inositol polyphosphate 1-phosphatase.” Proc Natl Acad Sci U S A 90, no. 12 (June 15, 1993): 5833–37. https://doi.org/10.1073/pnas.90.12.5833.Full Text Link to Item
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Neuwald, A. F., J. D. York, and P. W. Majerus. “Diverse proteins homologous to inositol monophosphatase.” Febs Lett 294, no. 1–2 (December 2, 1991): 16–18. https://doi.org/10.1016/0014-5793(91)81332-3.Full Text Link to Item
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Gu, M. X., J. D. York, I. Warshawsky, and P. W. Majerus. “Identification, cloning, and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1.” Proc Natl Acad Sci U S A 88, no. 13 (July 1, 1991): 5867–71. https://doi.org/10.1073/pnas.88.13.5867.Full Text Link to Item
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York, J. D., P. Li, and S. J. Gardell. “Combinatorial mutagenesis of the reactive site region in plasminogen activator inhibitor I.” J Biol Chem 266, no. 13 (May 5, 1991): 8495–8500.Link to Item
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York, J. D., and P. W. Majerus. “Isolation and heterologous expression of a cDNA encoding bovine inositol polyphosphate 1-phosphatase.” Proc Natl Acad Sci U S A 87, no. 24 (December 1990): 9548–52. https://doi.org/10.1073/pnas.87.24.9548.Full Text Link to Item
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Gardell, S. J., L. T. Duong, R. E. Diehl, J. D. York, T. R. Hare, R. B. Register, J. W. Jacobs, R. A. Dixon, and P. A. Friedman. “Isolation, characterization, and cDNA cloning of a vampire bat salivary plasminogen activator.” J Biol Chem 264, no. 30 (October 25, 1989): 17947–52.Link to Item
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Moseley, P. L., S. J. York, and J. York. “Bleomycin induces the hsp 70 heat shock promoter in cultured cells.” Am J Respir Cell Mol Biol 1, no. 2 (August 1989): 89–93. https://doi.org/10.1165/ajrcmb/1.2.89.Full Text Link to Item
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Book Sections
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York, J. D. “Inositol Polyphosphate Regulation of Nuclear Function.” In Handbook of Cell Signaling: Volume 1-3, 1–3:229–32, 2003. https://doi.org/10.1016/B978-012124546-7/50520-9.Full Text
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