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Identification of Fyn‐Induced PKA Binding Partners Using Quantitative Proteomics
Author(s) -
Weir Marion,
Mann Jacqueline,
Ballif Bryan,
Deming Paula
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.728.28
Subject(s) - fyn , stable isotope labeling by amino acids in cell culture , phosphorylation , chemistry , microbiology and biotechnology , kinase , serine , biochemistry , protein kinase a , signal transduction , tyrosine kinase , scaffold protein , threonine , proto oncogene tyrosine protein kinase src , proteomics , biology , gene
Protein Kinase A (PKA) is a serine/threonine kinase involved in many cellular processes including migration and proliferation. PKA is known to phosphorylate and activate members of the Src family of tyrosine kinases including Fyn, and new data from our laboratory indicate that Fyn can reciprocally regulate PKA. We hypothesized that co‐expression of Fyn with PKA would induce PKA to bind to and phosphorylate a distinct set of substrates such as scaffolding and signaling molecules. To test this, we used Stable Isotope Labeling of Amino Acids in Cell Culture (SILAC) and mass spectrometry to identify PKA binding partners that are dependent on the expression of Fyn. Several Fyn‐induced binding partners were identified. Further biochemical analyses have been performed for validation and characterization of these distinct signaling complexes.