Mass Spectrometry-Based Analysis of TRPP2 Phosphorylation.

Dumit, Verónica I; Köttgen, Michael; Hofherr, Alexis

Dumit, Verónica I; Köttgen, Michael; Hofherr, Alexis.

Afiliação

Dumit VI; Core Facility Proteomics, Center for Biological Systems Analysis (ZBSA), University of Freiburg, Freiburg, Germany.
Köttgen M; Renal Division, Department of Medicine, Faculty of Medicine, Medical Center, University of Freiburg, Freiburg, Germany.
Hofherr A; CIBSS - Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany.

Methods Mol Biol ; 1987: 51-64, 2019.

Article em En | MEDLINE | ID: mdl-31028673

ABSTRACT

ABSTRACT

Differential phosphorylation of proteins is a key regulatory mechanism in biology. Immunoprecipitation-coupled mass spectrometry facilitates the targeted analysis of transient receptor ion potential channel polycystin-2 (TRPP2) phosphorylation. However, empirical testing is required to optimize experimental conditions for immunoprecipitation and mass spectrometry. Here, we present a detailed workflow for the reliable analysis of endogenous TRPP2 phosphorylation in differentiated renal epithelial cells.

Assuntos

Espectrometria de Massas/métodos; Canais de Cátion TRPP/metabolismo; Animais; Células Epiteliais/enzimologia; Rim/enzimologia; Camundongos; Fosforilação; Canais de Cátion TRPP/química

Palavras-chave

ADPKD; Immunoprecipitation; Mass spectrometry; PKD2; Phosphoproteomics; Phosphorylation; Polycystic kidney disease; Post-translational modification; TRPP2

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Espectrometria de Massas / Canais de Cátion TRPP Limite: Animals Idioma: En Revista: Methods Mol Biol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Alemanha

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