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Methods for measuring RGS protein phosphorylation by G protein-regulated kinases.

Susanne Hollinger1, John R Hepler

  • 1Department of Pharmacology, Emory University School of Medicine, Atlanta, GA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|September 23, 2003
PubMed
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Regulators of G protein signaling (RGS) proteins, like RGS14, are phosphorylated by kinases. This study details methods to investigate RGS protein phosphorylation and its effects on function.

Area of Science:

  • Cellular signaling
  • Molecular biology
  • Protein biochemistry

Background:

  • Regulators of G protein signaling (RGS) proteins are key negative regulators of G protein signaling pathways.
  • Their cellular functions may extend beyond signal termination, necessitating an understanding of their regulation.
  • Kinase-mediated phosphorylation is a known regulatory mechanism for some RGS proteins, influencing their function and localization.

Purpose of the Study:

  • To investigate the cellular regulation of RGS proteins, focusing on RGS14 phosphorylation.
  • To outline laboratory protocols for studying RGS14 phosphorylation and purification.
  • To describe methods for identifying kinases that phosphorylate RGS proteins and the specific sites of modification.

Main Methods:

  • Purification of RGS14 protein.

Related Experiment Videos

  • Investigation of RGS14 recognition and phosphorylation by protein kinase A (PKA), extracellular signal-regulated kinase (ERK), and protein kinase C (PKC).
  • Strategies for identifying specific amino acid residues phosphorylated by these kinases.

    • Main Results:

    • Detailed protocols for RGS14 purification and phosphorylation studies are presented.
    • Methods for assessing RGS14 interaction with PKA, ERK, and PKC are described.
    • Techniques for pinpointing kinase-specific phosphorylation sites on RGS14 are outlined.

    Conclusions:

    • The study provides a methodological framework for investigating RGS protein phosphorylation.
    • Understanding RGS14 phosphorylation by specific kinases offers insights into broader RGS protein regulation.
    • The described protocols are adaptable for studying other RGS proteins.