Phospho serine and threonine analysis of normal and mutated granulocyte colony stimulating factor receptors.

Granulocyte colony stimulating factor receptor (G-CSFR) plays an important role in the production of neutrophil granulocytes. Mutated G-CSFRs have been directly associated with two distinct malignant phenotypes in patients, e.g. acute myeloid leukemia (AML) and chronic neutrophilic leukemia (CNL). However, the signaling mechanism of the mutated G-CSFRs is not well understood. Here, we present a comprehensive SILAC-based quantitative phosphoserine and phosphothreonine dataset of the normal and mutated G-CSFRs signaling using the BaF3 cell-line-based in vitro model system. High pH reversed phase concatenation and Titanium Dioxide Spin Tip column were utilized to increase the dynamic range and detection of the phosphoproteome of G-CSFRs. The dataset was further analyzed using several computational tools to validate the quality of the dataset. Overall, this dataset is the first global phosphoproteomics analysis of both normal and disease-associated-mutant G-CSFRs. We anticipate that this dataset will have a strong potential to decipher the phospho-signaling differences between the normal and malignant G-CSFR biology with therapeutic implications. The phosphoproteomic dataset is available via the PRIDE partner repository. Design Type(s) protein physical property analysis objective • replicate design • factorial design Measurement Type(s) protein expression profiling Technology Type(s) liquid chromatography-tandem mass spectrometry Factor Type(s) biological replicate • experimental condition Sample Characteristic(s) Mus musculus • BA/F3 cell Machine-accessible metadata file describing the reported data (ISA-Tab format) [ABSTRACT FROM AUTHOR]