Phosphoproteomics analysis of normal and mutated granulocyte colony stimulating factor receptors

Granulocyte colony stimulating factor receptor (G-CSFR) plays important role in the production of neutrophils from hematopoietic stem cells. Mutated form of the receptor has been directly associated with two distinct malignant phenotype 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 describe a comprehensive SILAC based quantitative phosphoproteomic analysis of the mutated G-CSFRs compared to the normal receptor using 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 and bioinformatics tools. Overall, this dataset is a first of any phosphoproteomics analysis of granulocyte colony stimulating factor receptors in the normal and disease associated mutations. We anticipate that our dataset will have a strong potential to decipher the phospho-signaling differences between the normal and malignant G-CSFR biology with therapeutic implications.