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Development of Selected Reaction Monitoring Methods to Systematically Quantify Kinase Abundance and Phosphorylation Stoichiometry in Human Samples.
Beck, Kirsten; Camp, Nathan; Bereman, Michael; Bollinger, James; Egertson, Jarrett; MacCoss, Michael; Wolf-Yadlin, Alejandro.
Afiliação
  • Beck K; Department of Genome Sciences, University of Washington, Seattle, WA, 98115, USA.
  • Camp N; Quintara Biosciences, San Francisco, CA, 94080, USA.
  • Bereman M; Center for Immunity and Immunotherapies, Seattle Children's Research Institute, Seattle, WA, USA.
  • Bollinger J; Department of Genome Sciences, University of Washington, Seattle, WA, 98115, USA.
  • Egertson J; North Carolina State University, Raleigh, NC, 27695, USA.
  • MacCoss M; Department of Genome Sciences, University of Washington, Seattle, WA, 98115, USA.
  • Wolf-Yadlin A; Washington University, St. Louis, MO, 63130, USA.
Methods Mol Biol ; 1636: 353-369, 2017.
Article em En | MEDLINE | ID: mdl-28730491
Protein phosphorylation, one of the most common types of post-translational modifications, is the central regulatory mechanism of cellular signaling networks. In human cells, thousands of proteins are continuously and dynamically phosphorylated and dephosphorylated at specific sites and times in response to external and internal stimuli. Reversible phosphorylation is facilitated by the action of two protein superfamilies: kinases and phosphatases. Kinases play an essential role in almost every relevant physiological process in human cells and their deregulation is linked to pathologies ranging from cancer to autoimmune diseases.Systematic identification of kinases expressed in a particular cell type, quantification of their abundance, and precise determination of their phosphorylation stoichiometry are essential to understand the cellular signaling networks and physiology of a sample. Our protocol outlines the steps to build and use a high-throughput, comprehensive, modular, and robust selected reaction monitoring (SRM) proteomics framework to facilitate quantification of the kinome state in research or clinical human samples.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fosfoproteínas / Proteínas Quinases / Proteoma / Proteômica Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fosfoproteínas / Proteínas Quinases / Proteoma / Proteômica Idioma: En Ano de publicação: 2017 Tipo de documento: Article