Alberto C Vitari

Summary

Affiliation: University of Dundee
Country: UK

Publications

  1. pmc WNK1, the kinase mutated in an inherited high-blood-pressure syndrome, is a novel PKB (protein kinase B)/Akt substrate
    Alberto C Vitari
    MRC Protein Phosphorylation Unit, School of Life Sciences, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
    Biochem J 378:257-68. 2004
  2. pmc The WNK1 and WNK4 protein kinases that are mutated in Gordon's hypertension syndrome phosphorylate and activate SPAK and OSR1 protein kinases
    Alberto C Vitari
    MRC Protein Phosphorylation Unit, School of Life Sciences, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
    Biochem J 391:17-24. 2005
  3. pmc Functional interactions of the SPAK/OSR1 kinases with their upstream activator WNK1 and downstream substrate NKCC1
    Alberto C Vitari
    MRC Protein Phosphorylation Unit, School of Life Sciences, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
    Biochem J 397:223-31. 2006
  4. pmc Regulation of activity and localization of the WNK1 protein kinase by hyperosmotic stress
    Anna Zagorska
    Medical Research Council Protein Phosphorylation Unit, School of Life Sciences, Medical Sciences Institute Wellcome Trust Biocentre Complex, University of Dundee, Dundee DD1 5EH, Scotland, UK
    J Cell Biol 176:89-100. 2007
  5. pmc SPAK/OSR1 regulate NKCC1 and WNK activity: analysis of WNK isoform interactions and activation by T-loop trans-autophosphorylation
    Jacob O Thastrup
    MRC Protein Phosphorylation Unit, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U K
    Biochem J 441:325-37. 2012

Collaborators

Detail Information

Publications5

  1. pmc WNK1, the kinase mutated in an inherited high-blood-pressure syndrome, is a novel PKB (protein kinase B)/Akt substrate
    Alberto C Vitari
    MRC Protein Phosphorylation Unit, School of Life Sciences, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
    Biochem J 378:257-68. 2004
    ..These results provide the first connection between the PI 3-kinase/PKB pathway and WNK1, suggesting a mechanism by which this pathway may influence blood pressure...
  2. pmc The WNK1 and WNK4 protein kinases that are mutated in Gordon's hypertension syndrome phosphorylate and activate SPAK and OSR1 protein kinases
    Alberto C Vitari
    MRC Protein Phosphorylation Unit, School of Life Sciences, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
    Biochem J 391:17-24. 2005
    ..Our analysis also describes the first facile assay that can be employed to quantitatively assess WNK1 and WNK4 activity...
  3. pmc Functional interactions of the SPAK/OSR1 kinases with their upstream activator WNK1 and downstream substrate NKCC1
    Alberto C Vitari
    MRC Protein Phosphorylation Unit, School of Life Sciences, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
    Biochem J 397:223-31. 2006
    ..These data establish that the CCT domain functions as a multipurpose docking site, enabling SPAK/OSR1 to interact with substrates (NKCC1) and activators (WNK1/WNK4)...
  4. pmc Regulation of activity and localization of the WNK1 protein kinase by hyperosmotic stress
    Anna Zagorska
    Medical Research Council Protein Phosphorylation Unit, School of Life Sciences, Medical Sciences Institute Wellcome Trust Biocentre Complex, University of Dundee, Dundee DD1 5EH, Scotland, UK
    J Cell Biol 176:89-100. 2007
    ..Mutational analysis suggests that the WNK1 C-terminal noncatalytic domain mediates vesicle localization. Our observations shed light on the mechanism by which WNK1 is regulated by hyperosmotic stress...
  5. pmc SPAK/OSR1 regulate NKCC1 and WNK activity: analysis of WNK isoform interactions and activation by T-loop trans-autophosphorylation
    Jacob O Thastrup
    MRC Protein Phosphorylation Unit, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U K
    Biochem J 441:325-37. 2012
    ..The knockin ES cells lacking SPAK/OSR1 activity will be useful in validating new targets of the WNK signalling pathway...