James T Murray

Summary

Affiliation: University of Dundee
Country: UK

Publications

  1. pmc Identification of filamin C as a new physiological substrate of PKBalpha using KESTREL
    James T Murray
    MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
    Biochem J 384:489-94. 2004
  2. pmc Exploitation of KESTREL to identify NDRG family members as physiological substrates for SGK1 and GSK3
    James T Murray
    MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
    Biochem J 384:477-88. 2004
  3. ncbi request reprint Identification of different specificity requirements between SGK1 and PKBalpha
    James T Murray
    MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
    FEBS Lett 579:991-4. 2005
  4. pmc mVps34 is activated following high-resistance contractions
    Matthew G Mackenzie
    James Black Centre, University of Dundee, Dundee, DD1 5EH, UK
    J Physiol 587:253-60. 2009
  5. ncbi request reprint hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase
    Maya P Byfield
    Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461, USA
    J Biol Chem 280:33076-82. 2005
  6. ncbi request reprint Analysis of hVps34/hVps15 interactions with Rab5 in vivo and in vitro
    James T Murray
    Methods Enzymol 403:789-99. 2005
  7. ncbi request reprint Role of Rab5 in the recruitment of hVps34/p150 to the early endosome
    James T Murray
    Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY, USA
    Traffic 3:416-27. 2002

Collaborators

Detail Information

Publications7

  1. pmc Identification of filamin C as a new physiological substrate of PKBalpha using KESTREL
    James T Murray
    MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
    Biochem J 384:489-94. 2004
    ..These results identify the muscle-specific isoform FLNc as a new physiological substrate for PKB...
  2. pmc Exploitation of KESTREL to identify NDRG family members as physiological substrates for SGK1 and GSK3
    James T Murray
    MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
    Biochem J 384:477-88. 2004
    ..Our results identify NDRG1 and NDRG2 as physiological substrates for SGK1, and demonstrate that phosphorylation of NDRG1 by SGK1 primes it for phosphorylation by GSK3...
  3. ncbi request reprint Identification of different specificity requirements between SGK1 and PKBalpha
    James T Murray
    MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
    FEBS Lett 579:991-4. 2005
    ..Our results identify a specific substrate for SGK1 and may facilitate detection of additional physiological substrates for this enzyme...
  4. pmc mVps34 is activated following high-resistance contractions
    Matthew G Mackenzie
    James Black Centre, University of Dundee, Dundee, DD1 5EH, UK
    J Physiol 587:253-60. 2009
    ..2-fold. These data suggest that, following high-resistance contractions, mVps34 activity is stimulated by an influx of essential amino acids such as leucine and this may prolong mTORC1 signalling and contribute to muscle hypertrophy...
  5. ncbi request reprint hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase
    Maya P Byfield
    Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461, USA
    J Biol Chem 280:33076-82. 2005
    ..Our data suggest that hVps34 is a nutrient-regulated lipid kinase that integrates amino acid and glucose inputs to mTOR and S6K1...
  6. ncbi request reprint Analysis of hVps34/hVps15 interactions with Rab5 in vivo and in vitro
    James T Murray
    Methods Enzymol 403:789-99. 2005
    ..This chapter describes the analysis of hVps34/hVps15 interactions with Rab5 in tissue culture cells and in vitro...
  7. ncbi request reprint Role of Rab5 in the recruitment of hVps34/p150 to the early endosome
    James T Murray
    Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY, USA
    Traffic 3:416-27. 2002
    ..However, Rab5 does not appear to act by directly recruiting p150/hVps34 complexes from the cytosol to the endosomal membrane...