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Updated: Jun 24, 2026
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Mass spectrometric identification of Rab23 phosphorylation as a response to challenge by cytidine 3',5'-cyclic
A Elizabeth Bond1, Edward Dudley, Robin Tuytten
1Biochemistry Group, Department of Biological Sciences, SOTEAS, Wallace Building, Swansea University, Singleton Park, Swansea SA2 8PP, UK.
Abstract:
While the functions and mechanisms of action of adenosine 3',5'-cyclic monophosphate (cAMP) and guanosine 3',5'-cyclic monophosphate (cGMP) are well established and are the basis of the action of a large number of successful pharmaceuticals, the role of a third naturally occurring cyclic nucleotide, cytidine 3',5'-cyclic monophosphate (cCMP), remains to be elucidated. Immobilized metal affinity chromatography (IMAC) was used to selectively extract proteins phosphorylated in mouse brain in response to challenge by cAMP, cGMP and cCMP, followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-ToFMS) and liquid chromatography/electrospray ionization tandem mass spectrometry (LC/ESI-MS/MS) of tryptic digests to identify Rab23 as the first protein reported to be phosphorylated only in response to cCMP.
