Development and application of a quantitative multiplexed small GTPase activity assay using targeted proteomics.

Cheng-Cheng Zhang, Ru Li, Honghui Jiang, Shujun Lin, Jason C Rogalski, Kate Liu, Juergen Kast
Author Information
  1. Cheng-Cheng Zhang: The Biomedical Research Centre, ∥The Centre for Blood Research, University of British Columbia , Vancouver, BC V6T 1Z3, Canada.

Abstract

Small GTPases are a family of key signaling molecules that are ubiquitously expressed in various types of cells. Their activity is often analyzed by western blot, which is limited by its multiplexing capability, the quality of isoform-specific antibodies, and the accuracy of quantification. To overcome these issues, a quantitative multiplexed small GTPase activity assay has been developed. Using four different binding domains, this assay allows the binding of up to 12 active small GTPase isoforms simultaneously in a single experiment. To accurately quantify the closely related small GTPase isoforms, a targeted proteomic approach, i.e., selected/multiple reaction monitoring, was developed, and its functionality and reproducibility were validated. This assay was successfully applied to human platelets and revealed time-resolved coactivation of multiple small GTPase isoforms in response to agonists and differential activation of these isoforms in response to inhibitor treatment. This widely applicable approach can be used for signaling pathway studies and inhibitor screening in many cellular systems.

Keywords

Grants

  1. /Canadian Institutes of Health Research

MeSH Term

Blood Platelets
Cells, Cultured
Chromatography, Reverse-Phase
GTP Phosphohydrolase Activators
Humans
Isotope Labeling
Peptide Fragments
Platelet Activation
Protein Isoforms
Proteomics
Reproducibility of Results
Tandem Mass Spectrometry

Chemicals

GTP Phosphohydrolase Activators
Peptide Fragments
Protein Isoforms

Word Cloud

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