J C Lawrence

Summary

Affiliation: University of Virginia
Country: USA

Publications

  1. ncbi request reprint Control of the translational regulators PHAS-I and PHAS-II by insulin and cAMP in 3T3-L1 adipocytes
    T A Lin
    Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St Louis, Missouri 63110, USA
    J Biol Chem 271:30199-204. 1996
  2. ncbi request reprint New insights into the role and mechanism of glycogen synthase activation by insulin
    J C Lawrence
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22908, USA
    Diabetes 46:541-7. 1997
  3. pmc Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression
    I Mothe-Satney
    Departments of Pharmacology, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA
    Mol Cell Biol 20:3558-67. 2000
  4. ncbi request reprint Mammalian target of rapamycin-dependent phosphorylation of PHAS-I in four (S/T)P sites detected by phospho-specific antibodies
    I Mothe-Satney
    Departments of Pharmacology and Medicine, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA
    J Biol Chem 275:33836-43. 2000
  5. ncbi request reprint Identification of phosphorylation sites in the translational regulator, PHAS-I, that are controlled by insulin and rapamycin in rat adipocytes
    P Fadden
    Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA
    J Biol Chem 272:10240-7. 1997
  6. ncbi request reprint PHAS proteins as mediators of the actions of insulin, growth factors and cAMP on protein synthesis and cell proliferation
    J C Lawrence
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22908, USA
    Adv Enzyme Regul 37:239-67. 1997
  7. ncbi request reprint Mutational analysis of sites in the translational regulator, PHAS-I, that are selectively phosphorylated by mTOR
    D Yang
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22908, USA
    FEBS Lett 453:387-90. 1999
  8. ncbi request reprint The mammalian target of rapamycin phosphorylates sites having a (Ser/Thr)-Pro motif and is activated by antibodies to a region near its COOH terminus
    G J Brunn
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA
    J Biol Chem 272:32547-50. 1997
  9. ncbi request reprint Modulation of the protein kinase activity of mTOR
    J C Lawrence
    Department of Pharmacology, University of Virginia School of Medicine, 1300 Jefferson Park Avenue, Charlottesville, VA 22908 0735, USA
    Curr Top Microbiol Immunol 279:199-213. 2004
  10. ncbi request reprint Phosphorylation of PHAS-I by mitogen-activated protein (MAP) kinase. Identification of a site phosphorylated by MAP kinase in vitro and in response to insulin in rat adipocytes
    T A Haystead
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22903
    J Biol Chem 269:23185-91. 1994

Collaborators

Detail Information

Publications20

  1. ncbi request reprint Control of the translational regulators PHAS-I and PHAS-II by insulin and cAMP in 3T3-L1 adipocytes
    T A Lin
    Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St Louis, Missouri 63110, USA
    J Biol Chem 271:30199-204. 1996
    ..In summary, our results indicate that PHAS-I and -II are controlled by the mammalian target of rapamycin and p70(S6K) signaling pathway and that in 3T3-L1 adipocytes this pathway is inhibited by increased cAMP...
  2. ncbi request reprint New insights into the role and mechanism of glycogen synthase activation by insulin
    J C Lawrence
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22908, USA
    Diabetes 46:541-7. 1997
    ..Though promising, this model still does not completely explain the molecular basis for the insulin-mediated activation of glycogen synthase, which remains one of the many unknowns of insulin action...
  3. pmc Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression
    I Mothe-Satney
    Departments of Pharmacology, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA
    Mol Cell Biol 20:3558-67. 2000
    ..However, each of the sites influences mRNA translation, either directly by modulating the binding affinity of PHAS-I and eIF4E or indirectly by affecting the phosphorylation of other sites...
  4. ncbi request reprint Mammalian target of rapamycin-dependent phosphorylation of PHAS-I in four (S/T)P sites detected by phospho-specific antibodies
    I Mothe-Satney
    Departments of Pharmacology and Medicine, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA
    J Biol Chem 275:33836-43. 2000
    ..In these respects the phosphorylation of PHAS-I by mTOR in vitro resembles the ordered phosphorylation of PHAS-I in cells...
  5. ncbi request reprint Identification of phosphorylation sites in the translational regulator, PHAS-I, that are controlled by insulin and rapamycin in rat adipocytes
    P Fadden
    Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA
    J Biol Chem 272:10240-7. 1997
    ..All five sites identified fit a (Ser/Thr)-Pro motif, suggesting that the phosphorylation of PHAS-I in cells is mediated by a proline-directed protein kinase...
  6. ncbi request reprint PHAS proteins as mediators of the actions of insulin, growth factors and cAMP on protein synthesis and cell proliferation
    J C Lawrence
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22908, USA
    Adv Enzyme Regul 37:239-67. 1997
    ..Pharmacological and genetic evidence indicates that the mTOR/p70S6K pathway is involved in the control of PHAS-I and -II. Thus, PHAS proteins may be mediators of the effects of this pathway on protein synthesis and cell proliferation...
  7. ncbi request reprint Mutational analysis of sites in the translational regulator, PHAS-I, that are selectively phosphorylated by mTOR
    D Yang
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22908, USA
    FEBS Lett 453:387-90. 1999
    ..Phosphorylation of neither site affected the electrophoretic mobility of the protein, indicating that results of studies that rely solely on a gel-shift assay to assess changes in PHAS-I phosphorylation must be interpreted with caution...
  8. ncbi request reprint The mammalian target of rapamycin phosphorylates sites having a (Ser/Thr)-Pro motif and is activated by antibodies to a region near its COOH terminus
    G J Brunn
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA
    J Biol Chem 272:32547-50. 1997
    ..Thus, our findings indicate that Pro is a determinant of the mTOR protein kinase specificity and that mTOR contributes to the phosphorylation of PHAS-I in cells...
  9. ncbi request reprint Modulation of the protein kinase activity of mTOR
    J C Lawrence
    Department of Pharmacology, University of Virginia School of Medicine, 1300 Jefferson Park Avenue, Charlottesville, VA 22908 0735, USA
    Curr Top Microbiol Immunol 279:199-213. 2004
    ....
  10. ncbi request reprint Phosphorylation of PHAS-I by mitogen-activated protein (MAP) kinase. Identification of a site phosphorylated by MAP kinase in vitro and in response to insulin in rat adipocytes
    T A Haystead
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22903
    J Biol Chem 269:23185-91. 1994
    ..We conclude that PHAS-I is a substrate for MAP kinase both in vivo and in vitro. As PHAS-I is one of the most prominent insulin-stimulated phosphoproteins in adipocytes, it may qualify as the major MAP kinase substrate in these cells...
  11. ncbi request reprint PHAS-I as a link between mitogen-activated protein kinase and translation initiation
    T A Lin
    Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St Louis, MO 63110
    Science 266:653-6. 1994
    ..Thus, PHAS-I may be a key mediator of the stimulation of protein synthesis by the diverse group of agents and stimuli that activate MAP kinase...
  12. ncbi request reprint mTOR-dependent control of skeletal muscle protein synthesis
    J C Lawrence
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22908, USA
    Int J Sport Nutr Exerc Metab 11:S177-85. 2001
    ..Recently, significant progress has been made in understanding the biochemical mechanisms that control the rate of translation initiation, which is generally the limiting phase in protein synthesis...
  13. ncbi request reprint Control of PHAS-I by insulin in 3T3-L1 adipocytes. Synthesis, degradation, and phosphorylation by a rapamycin-sensitive and mitogen-activated protein kinase-independent pathway
    T A Lin
    Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St Louis, Missouri 63110, USA
    J Biol Chem 270:18531-8. 1995
    ..Rapamycin may inhibit translation initiation by increasing PHAS-I binding to eIF-4E...
  14. pmc Molecular cloning and tissue distribution of PHAS-I, an intracellular target for insulin and growth factors
    C Hu
    Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St Louis, MO 63110
    Proc Natl Acad Sci U S A 91:3730-4. 1994
    ..However, in view of its tissue distribution and the fact that the protein is phosphorylated in response to insulin, we speculate that PHAS-I is important in insulin action...
  15. ncbi request reprint PHAS/4E-BPs as regulators of mRNA translation and cell proliferation
    J C Lawrence
    Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22908, USA
    Trends Biochem Sci 22:345-9. 1997
    ..PHAS/4E-BPs, a recently discovered family of elF4E-binding, proteins, appear to play a key role in this process, as well as in the control of cell proliferation...
  16. ncbi request reprint Control of glycogen synthesis is shared between glucose transport and glycogen synthase in skeletal muscle fibers
    I Azpiazu
    Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St Louis, Missouri 63110, USA
    Am J Physiol Endocrinol Metab 278:E234-43. 2000
    ....
  17. ncbi request reprint Phosphorylase kinase isozymes and phosphorylase in denervated skeletal muscles
    J C Lawrence
    Department of Pharmacology, Washington University School of Medicine, St Louis, MO 63110
    Muscle Nerve 13:133-7. 1990
    ..The decreases in these enzymes explain, at least in part, the marked alterations in glycogen metabolism that occur after motor denervation...
  18. ncbi request reprint Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function
    A Pause
    Department of Biochemistry, McGill University, Montreal, Quebec, Canada
    Nature 371:762-7. 1994
    ..The action of this new regulator of protein synthesis is therefore modulated by insulin, which acts to stimulate the overall rate of translation and promote cell growth...
  19. ncbi request reprint Disruption of the gene encoding the mitogen-regulated translational modulator PHAS-I in mice
    P J Blackshear
    Department of Medicine, The Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 272:31510-4. 1997
    ....
  20. pmc Insulin control of glycogen metabolism in knockout mice lacking the muscle-specific protein phosphatase PP1G/RGL
    Y Suzuki
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202
    Mol Cell Biol 21:2683-94. 2001
    ..However, PP1G/RGL is not required for insulin activation of GS in skeletal muscle, and rather another GS-specific phosphatase appears to be involved...